https://proteopedia.org/index.php?action=history&feed=atom&title=DomainDomain - Revision history2026-10-01T23:40:01ZRevision history for this page on the wikiMediaWiki 1.43.8https://proteopedia.org/index.php?title=Domain&diff=3361039&oldid=prevEric Martz at 19:07, 28 February 20212021-02-28T19:07:43Z<p></p>
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<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>* [[2hhd]]: Each of the 4 chains that form hemoglobin (a tetramer) folds into a single domain composed of alpha-helices. Each domain (chain) is 141-146 amino acids in length for human hemoglobin.</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>* [[2hhd]]: Each of the 4 chains that form hemoglobin (a tetramer) folds into a single domain composed of alpha-helices. Each domain (chain) is 141-146 amino acids in length for human hemoglobin.</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>* [[1igy]]: Immunoglobulin G (antibody) consists of 12 domains in 4 chains. These domains are composed of beta-sheets. Each of the two heavy chains has 4 domains, and each of the 2 light chains has 2 domains. These domains are about 110 amino acids in length. Each heavy chain has two pairs of domains connected by a flexible linker about 20 amino acids in length.</div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>* [[1igy]]: Immunoglobulin G (antibody) consists of 12 domains in 4 chains. These <ins style="font-weight: bold; text-decoration: none;">''immunoglobulin superfamily'' </ins>domains are composed of beta-sheets. Each of the two heavy chains has 4 domains, and each of the 2 light chains has 2 domains. These domains are about 110 amino acids in length. Each heavy chain has two pairs of domains connected by a flexible linker about 20 amino acids in length.</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>For more information see [http://www.wikipedia.com/wiki/Protein_domain Protein Domain in Wikipedia].</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>For more information see [http://www.wikipedia.com/wiki/Protein_domain Protein Domain in Wikipedia].</div></td></tr>
</table>Eric Martzhttps://proteopedia.org/index.php?title=Domain&diff=3361036&oldid=prevEric Martz at 19:04, 28 February 20212021-02-28T19:04:33Z<p></p>
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<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>A protein ''domain'' usually means a sequence of amino acids that folds, independently of the remainder of the full-length sequence, into a compact stable structure. Water-soluble domains typically have hydrophobic cores. Some small full-length proteins consist of a single domain, but <del style="font-weight: bold; text-decoration: none;">most </del>proteins have two or more domains. A domain is typically 100-250 amino acids in length<ref name="EPR" />, but can sometimes be shorter or longer.</div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>A protein ''domain'' usually means a sequence of amino acids that folds, independently of the remainder of the full-length sequence, into a compact stable structure. Water-soluble domains typically have hydrophobic cores. Some small full-length proteins consist of a single domain, but <ins style="font-weight: bold; text-decoration: none;">many </ins>proteins have two or more domains. A domain is typically 100-250 amino acids in length<ref name="EPR" />, but can sometimes be shorter or longer.</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>In 2006, chains with a single domain in the CATH database had an average length of 159<ref name="cath2006">PMID: 17135200</ref>.</div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>In 2006, chains with a single domain in the CATH database had an average length of 159<ref name="cath2006">PMID: 17135200</ref<ins style="font-weight: bold; text-decoration: none;">>. In 2006, 64% of all protein structures in CATH were single domain chains. 27% were two-domain chains<ref name="cath2006" /</ins>>.</div></td></tr>
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</table>Eric Martzhttps://proteopedia.org/index.php?title=Domain&diff=3361035&oldid=prevEric Martz at 19:02, 28 February 20212021-02-28T19:02:25Z<p></p>
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<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>A protein ''domain'' usually means a sequence of amino acids that folds, independently of the remainder of the full-length sequence, into a compact stable structure. Water-soluble domains typically have hydrophobic cores. Some small full-length proteins consist of a single domain, but most proteins have two or more domains. A domain is typically 100-250 amino acids in length<ref name="EPR" />, but can sometimes be shorter or longer.</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>A protein ''domain'' usually means a sequence of amino acids that folds, independently of the remainder of the full-length sequence, into a compact stable structure. Water-soluble domains typically have hydrophobic cores. Some small full-length proteins consist of a single domain, but most proteins have two or more domains. A domain is typically 100-250 amino acids in length<ref name="EPR" />, but can sometimes be shorter or longer.</div></td></tr>
<tr><td colspan="2" class="diff-side-deleted"></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div><ins style="font-weight: bold; text-decoration: none;"></ins></div></td></tr>
<tr><td colspan="2" class="diff-side-deleted"></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div><ins style="font-weight: bold; text-decoration: none;">In 2006, chains with a single domain in the CATH database had an average length of 159<ref name="cath2006">PMID: 17135200</ref>.</ins></div></td></tr>
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</table>Eric Martzhttps://proteopedia.org/index.php?title=Domain&diff=2988301&oldid=prevEric Martz at 21:06, 5 January 20192019-01-05T21:06:38Z<p></p>
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<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>A protein ''domain'' <del style="font-weight: bold; text-decoration: none;">is </del>a sequence of amino acids that folds, independently of the remainder of the full-length sequence, into a compact stable structure. Water-soluble domains typically have hydrophobic cores. Some small full-length proteins consist of a single domain, but most proteins have two or more domains. A domain is typically 100-250 amino acids in length<ref name="EPR" />, but can sometimes be shorter or longer.</div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>A protein ''domain'' <ins style="font-weight: bold; text-decoration: none;">usually means </ins>a sequence of amino acids that folds, independently of the remainder of the full-length sequence, into a compact stable structure. Water-soluble domains typically have hydrophobic cores. Some small full-length proteins consist of a single domain, but most proteins have two or more domains. A domain is typically 100-250 amino acids in length<ref name="EPR" />, but can sometimes be shorter or longer.</div></td></tr>
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</table>Eric Martzhttps://proteopedia.org/index.php?title=Domain&diff=2926793&oldid=prevEric Martz at 20:33, 19 July 20182018-07-19T20:33:47Z<p></p>
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<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>* [[9ins]] (porcine): Insulin, with 51 amino acids, is one of the smallest stably folded protein domains, on the boundary between a protein and a [[peptide]]. It has a hydrophobic core. Human preproinsulin is synthesized with 110 amino acids. After removal of a 24 amino acid signal sequence, the remaining 86 amino acid proinsulin is cleaved in two places, forming a mature disulfide-linked dimer of two protein chains. Chain B is residues 1-30. Chain A is residues 66-86 (length 21). "C-peptide", residues 33-63 (length 31), is released as a separate bio-active peptide. Mature human insulin differs from porcine in a single amino acid: the terminal residue in chain B is Thr vs. Ala, respectively. Wikipedia has good articles on [https://en.wikipedia.org/wiki/Insulin#Synthesis insulin synthesis] and [https://en.wikipedia.org/wiki/C-peptide C-peptide]. See also [[Insulin Structure & Function]].</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>* [[9ins]] (porcine): Insulin, with 51 amino acids, is one of the smallest stably folded protein domains, on the boundary between a protein and a [[peptide]]. It has a hydrophobic core. Human preproinsulin is synthesized with 110 amino acids. After removal of a 24 amino acid signal sequence, the remaining 86 amino acid proinsulin is cleaved in two places, forming a mature disulfide-linked dimer of two protein chains. Chain B is residues 1-30. Chain A is residues 66-86 (length 21). "C-peptide", residues 33-63 (length 31), is released as a separate bio-active peptide. Mature human insulin differs from porcine in a single amino acid: the terminal residue in chain B is Thr vs. Ala, respectively. Wikipedia has good articles on [https://en.wikipedia.org/wiki/Insulin#Synthesis insulin synthesis] and [https://en.wikipedia.org/wiki/C-peptide C-peptide]. See also [[Insulin Structure & Function]].</div></td></tr>
<tr><td colspan="2" class="diff-side-deleted"></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div><ins style="font-weight: bold; text-decoration: none;"></ins></div></td></tr>
<tr><td colspan="2" class="diff-side-deleted"></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div><ins style="font-weight: bold; text-decoration: none;">* [[1lzs]]: Lysozyme functions as a single chain of 130 amino acids. It folds to single domain with a hydrophobic core.</ins></div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>* [[2hhd]]: Each of the 4 chains that form hemoglobin (a tetramer) folds into a single domain composed of alpha-helices. Each domain (chain) is 141-146 amino acids in length for human hemoglobin.</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>* [[2hhd]]: Each of the 4 chains that form hemoglobin (a tetramer) folds into a single domain composed of alpha-helices. Each domain (chain) is 141-146 amino acids in length for human hemoglobin.</div></td></tr>
</table>Eric Martzhttps://proteopedia.org/index.php?title=Domain&diff=2926792&oldid=prevEric Martz at 20:22, 19 July 20182018-07-19T20:22:40Z<p></p>
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 20:22, 19 July 2018</td>
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<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>Examples:</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>Examples:</div></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>* [[9ins]]: Insulin, with 51 amino acids, is one of the smallest stably folded protein domains, on the boundary between a protein and a [[peptide]]. It has a hydrophobic core. Human preproinsulin is synthesized with 110 amino acids. After removal of a 24 amino acid signal sequence, the remaining 86 amino acid proinsulin is cleaved in two places, forming a mature disulfide-linked dimer of two protein chains. Chain B is residues 1-30. Chain A is residues 66-86 (length 21). "C-peptide", residues 33-63 (length 31), is released as a separate bio-active peptide. Wikipedia has good articles on [https://en.wikipedia.org/wiki/Insulin#Synthesis insulin synthesis] and [https://en.wikipedia.org/wiki/C-peptide C-peptide]. See also [[Insulin Structure & Function]].</div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>* [[9ins]] <ins style="font-weight: bold; text-decoration: none;">(porcine)</ins>: Insulin, with 51 amino acids, is one of the smallest stably folded protein domains, on the boundary between a protein and a [[peptide]]. It has a hydrophobic core. Human preproinsulin is synthesized with 110 amino acids. After removal of a 24 amino acid signal sequence, the remaining 86 amino acid proinsulin is cleaved in two places, forming a mature disulfide-linked dimer of two protein chains. Chain B is residues 1-30. Chain A is residues 66-86 (length 21). "C-peptide", residues 33-63 (length 31), is released as a separate bio-active peptide<ins style="font-weight: bold; text-decoration: none;">. Mature human insulin differs from porcine in a single amino acid: the terminal residue in chain B is Thr vs. Ala, respectively</ins>. Wikipedia has good articles on [https://en.wikipedia.org/wiki/Insulin#Synthesis insulin synthesis] and [https://en.wikipedia.org/wiki/C-peptide C-peptide]. See also [[Insulin Structure & Function]].</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>* [[2hhd]]: Each of the 4 chains that form hemoglobin (a tetramer) folds into a single domain composed of alpha-helices. Each domain (chain) is 141-146 amino acids in length for human hemoglobin.</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>* [[2hhd]]: Each of the 4 chains that form hemoglobin (a tetramer) folds into a single domain composed of alpha-helices. Each domain (chain) is 141-146 amino acids in length for human hemoglobin.</div></td></tr>
</table>Eric Martzhttps://proteopedia.org/index.php?title=Domain&diff=2926791&oldid=prevEric Martz at 20:06, 19 July 20182018-07-19T20:06:25Z<p></p>
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 20:06, 19 July 2018</td>
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<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>Examples:</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>Examples:</div></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>* [[9ins]]: Insulin, with 51 amino acids, is one of the smallest stably folded protein domains, on the boundary between a protein and a [[peptide]]. It has a hydrophobic core. Human preproinsulin is synthesized with 110 amino acids. After removal of a 24 amino acid signal sequence, the remaining 86 amino acid proinsulin is cleaved in two places, forming a mature disulfide-linked dimer of two protein chains. Chain B is residues 1-30. Chain A is residues 66-86 (length 21). "C-peptide", residues 33-63 (length 31), is released as a separate bio-active peptide. Wikipedia has good articles on [https://en.wikipedia.org/wiki/Insulin#Synthesis insulin synthesis] and [https://en.wikipedia.org/wiki/C-peptide C-peptide].</div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>* [[9ins]]: Insulin, with 51 amino acids, is one of the smallest stably folded protein domains, on the boundary between a protein and a [[peptide]]. It has a hydrophobic core. Human preproinsulin is synthesized with 110 amino acids. After removal of a 24 amino acid signal sequence, the remaining 86 amino acid proinsulin is cleaved in two places, forming a mature disulfide-linked dimer of two protein chains. Chain B is residues 1-30. Chain A is residues 66-86 (length 21). "C-peptide", residues 33-63 (length 31), is released as a separate bio-active peptide. Wikipedia has good articles on [https://en.wikipedia.org/wiki/Insulin#Synthesis insulin synthesis] and [https://en.wikipedia.org/wiki/C-peptide C-peptide<ins style="font-weight: bold; text-decoration: none;">]. See also [[Insulin Structure & Function]</ins>].</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>* [[2hhd]]: Each of the 4 chains that form hemoglobin (a tetramer) folds into a single domain composed of alpha-helices. Each domain (chain) is 141-146 amino acids in length for human hemoglobin.</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>* [[2hhd]]: Each of the 4 chains that form hemoglobin (a tetramer) folds into a single domain composed of alpha-helices. Each domain (chain) is 141-146 amino acids in length for human hemoglobin.</div></td></tr>
</table>Eric Martzhttps://proteopedia.org/index.php?title=Domain&diff=2926790&oldid=prevEric Martz at 20:02, 19 July 20182018-07-19T20:02:54Z<p></p>
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 20:02, 19 July 2018</td>
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<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>Examples:</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>Examples:</div></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>* [[9ins]]: Insulin, with 51 amino acids, is one of the smallest stably folded protein domains, on the boundary between a protein and a [[peptide]]. It has a hydrophobic core. <del style="font-weight: bold; text-decoration: none;">Preproinsulin </del>is synthesized with 110 amino acids. After removal of a 24 amino acid signal sequence, the remaining <del style="font-weight: bold; text-decoration: none;">84 </del>amino acid proinsulin is cleaved in two places, forming a mature disulfide-linked dimer of two protein chains. Chain B is residues 1-30. Chain A is residues 66-86 (length 21).</div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>* [[9ins]]: Insulin, with 51 amino acids, is one of the smallest stably folded protein domains, on the boundary between a protein and a [[peptide]]. It has a hydrophobic core. <ins style="font-weight: bold; text-decoration: none;">Human preproinsulin </ins>is synthesized with 110 amino acids. After removal of a 24 amino acid signal sequence, the remaining <ins style="font-weight: bold; text-decoration: none;">86 </ins>amino acid proinsulin is cleaved in two places, forming a mature disulfide-linked dimer of two protein chains. Chain B is residues 1-30. Chain A is residues 66-86 (length 21)<ins style="font-weight: bold; text-decoration: none;">. "C-peptide", residues 33-63 (length 31), is released as a separate bio-active peptide. Wikipedia has good articles on [https://en.wikipedia.org/wiki/Insulin#Synthesis insulin synthesis] and [https://en.wikipedia.org/wiki/C-peptide C-peptide]</ins>.</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>* [[2hhd]]: Each of the 4 chains that form hemoglobin (a tetramer) folds into a single domain composed of alpha-helices. Each domain (chain) is 141-146 amino acids in length for human hemoglobin.</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>* [[2hhd]]: Each of the 4 chains that form hemoglobin (a tetramer) folds into a single domain composed of alpha-helices. Each domain (chain) is 141-146 amino acids in length for human hemoglobin.</div></td></tr>
</table>Eric Martzhttps://proteopedia.org/index.php?title=Domain&diff=2926789&oldid=prevEric Martz at 19:58, 19 July 20182018-07-19T19:58:44Z<p></p>
<table style="background-color: #fff; color: #202122;" data-mw="interface">
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 19:58, 19 July 2018</td>
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<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>Examples:</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>Examples:</div></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>* [[9ins]]: Insulin, with 51 amino acids, is one of the smallest stably folded protein domains, on the boundary between a protein and a [[peptide]]. It has a hydrophobic core. Preproinsulin is synthesized <del style="font-weight: bold; text-decoration: none;">as 108 </del>amino acids. After removal of a 24 amino acid signal sequence, the remaining 84 amino acid proinsulin is cleaved in two places, forming a disulfide-linked dimer of two protein chains <del style="font-weight: bold; text-decoration: none;">of 21 and </del>30 residues (<del style="font-weight: bold; text-decoration: none;">total: 51</del>).</div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>* [[9ins]]: Insulin, with 51 amino acids, is one of the smallest stably folded protein domains, on the boundary between a protein and a [[peptide]]. It has a hydrophobic core. Preproinsulin is synthesized <ins style="font-weight: bold; text-decoration: none;">with 110 </ins>amino acids. After removal of a 24 amino acid signal sequence, the remaining 84 amino acid proinsulin is cleaved in two places, forming a <ins style="font-weight: bold; text-decoration: none;">mature </ins>disulfide-linked dimer of two protein chains<ins style="font-weight: bold; text-decoration: none;">. Chain B is residues 1-</ins>30<ins style="font-weight: bold; text-decoration: none;">. Chain A is </ins>residues <ins style="font-weight: bold; text-decoration: none;">66-86 </ins>(<ins style="font-weight: bold; text-decoration: none;">length 21</ins>).</div></td></tr>
<tr><td colspan="2" class="diff-side-deleted"></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div> </div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>* [[2hhd]]: Each of the 4 chains that form hemoglobin (a tetramer) folds into a single domain composed of alpha-helices. Each domain (chain) is 141-146 amino acids in length for human hemoglobin.</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>* [[2hhd]]: Each of the 4 chains that form hemoglobin (a tetramer) folds into a single domain composed of alpha-helices. Each domain (chain) is 141-146 amino acids in length for human hemoglobin.</div></td></tr>
<tr><td colspan="2" class="diff-side-deleted"></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div><ins style="font-weight: bold; text-decoration: none;"></ins></div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>* [[1igy]]: Immunoglobulin G (antibody) consists of 12 domains in 4 chains. These domains are composed of beta-sheets. Each of the two heavy chains has 4 domains, and each of the 2 light chains has 2 domains. These domains are about 110 amino acids in length. Each heavy chain has two pairs of domains connected by a flexible linker about 20 amino acids in length.</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>* [[1igy]]: Immunoglobulin G (antibody) consists of 12 domains in 4 chains. These domains are composed of beta-sheets. Each of the two heavy chains has 4 domains, and each of the 2 light chains has 2 domains. These domains are about 110 amino acids in length. Each heavy chain has two pairs of domains connected by a flexible linker about 20 amino acids in length.</div></td></tr>
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</table>Eric Martzhttps://proteopedia.org/index.php?title=Domain&diff=2926788&oldid=prevEric Martz at 19:51, 19 July 20182018-07-19T19:51:51Z<p></p>
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 19:51, 19 July 2018</td>
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<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>Examples:</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>Examples:</div></td></tr>
<tr><td colspan="2" class="diff-side-deleted"></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div><ins style="font-weight: bold; text-decoration: none;">* [[9ins]]: Insulin, with 51 amino acids, is one of the smallest stably folded protein domains, on the boundary between a protein and a [[peptide]]. It has a hydrophobic core. Preproinsulin is synthesized as 108 amino acids. After removal of a 24 amino acid signal sequence, the remaining 84 amino acid proinsulin is cleaved in two places, forming a disulfide-linked dimer of two protein chains of 21 and 30 residues (total: 51).</ins></div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>* [[2hhd]]: Each of the 4 chains that form hemoglobin (a tetramer) folds into a single domain composed of alpha-helices. Each domain (chain) is 141-146 amino acids in length for human hemoglobin.</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>* [[2hhd]]: Each of the 4 chains that form hemoglobin (a tetramer) folds into a single domain composed of alpha-helices. Each domain (chain) is 141-146 amino acids in length for human hemoglobin.</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>* [[1igy]]: Immunoglobulin G (antibody) consists of 12 domains in 4 chains. These domains are composed of beta-sheets. Each of the two heavy chains has 4 domains, and each of the 2 light chains has 2 domains. These domains are about 110 amino acids in length. Each heavy chain has two pairs of domains connected by a flexible linker about 20 amino acids in length.</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>* [[1igy]]: Immunoglobulin G (antibody) consists of 12 domains in 4 chains. These domains are composed of beta-sheets. Each of the two heavy chains has 4 domains, and each of the 2 light chains has 2 domains. These domains are about 110 amino acids in length. Each heavy chain has two pairs of domains connected by a flexible linker about 20 amino acids in length.</div></td></tr>
</table>Eric Martz