Domain: Difference between revisions

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Examples:

* [[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 with 110 amino acids. After removal of a 24 amino acid signal sequence, the remaining 84 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).

* [[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].

* [[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.

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 Examples:
-* [[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 with 110 amino acids. After removal of a 24 amino acid signal sequence, the remaining 84 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).
+* [[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].
 * [[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.