Sandbox Reserved 1121: Difference between revisions

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=== CRP structure ===

Ser53, His95, Cys97, Asp112, Gly113, Gly136, Gly154, Val165, Leu166, Ile171, and Gly196 are the highly conserved residues in the primary sequence of CRP <ref name="kumar"/>.

The C-reactive protein is a homopentamer of non-covalently bound subunits. Each subunit is a 25 Da protein consisting of 224 residues bound together. The secondary structure is formed of one <scene name='71/719862/Helix/1'>α-helix</scene> and two antiparallel β-sheets <ref>[http://www.uniprot.org/uniprot/P02741 UniProtKB - P02741 (CRP_HUMAN)]</ref>. The predominant structure is β-sheet <ref>PMID: 1382589</ref> but short helical regions can be noticed for the residues 43 and 185 <ref name="kumar"/>. The residues Glu197 and Lys123 of CRP form an intermolecular ion pair <ref name="thompson">PMID: 10368284</ref>.

The C-reactive protein is a homopentamer of non-covalently bound subunits. Each subunit is a 25 Da protein consisting of 224 residues bound together. The secondary structure is formed of one <scene name='71/719862/Helix/1'>α-helix</scene> and two antiparallel <scene name='71/719862/Sheet/1'>β-sheets</scene> <ref>[http://www.uniprot.org/uniprot/P02741 UniProtKB - P02741 (CRP_HUMAN)]</ref>. The predominant structure is β-sheet <ref>PMID: 1382589</ref> but short helical regions can be noticed for the residues 43 and 185 <ref name="kumar"/>. The residues Glu197 and Lys123 of CRP form an intermolecular ion pair <ref name="thompson">PMID: 10368284</ref>.

The diameter of the CRP pentamer is 102 Å, the inner pore diameter is 30 Å and the diameter of a subunit is 36 Å <ref name="agrawal">PMID: 19799114 </ref>.

Sandbox Reserved 1121: Difference between revisions

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 === CRP structure ===
 Ser53, His95, Cys97, Asp112, Gly113, Gly136, Gly154, Val165, Leu166, Ile171, and Gly196 are the highly conserved residues in the primary sequence of CRP <ref name="kumar"/>.
-The C-reactive protein is a homopentamer of non-covalently bound subunits. Each subunit is a 25 Da protein consisting of 224 residues bound together. The secondary structure is formed of one <scene name='71/719862/Helix/1'>α-helix</scene> and two antiparallel β-sheets <ref>[http://www.uniprot.org/uniprot/P02741 UniProtKB - P02741 (CRP_HUMAN)]</ref>. The predominant structure is β-sheet <ref>PMID: 1382589</ref> but short helical regions can be noticed for the residues 43 and 185 <ref name="kumar"/>. The residues Glu197 and Lys123 of CRP form an intermolecular ion pair <ref name="thompson">PMID: 10368284</ref>.
+The C-reactive protein is a homopentamer of non-covalently bound subunits. Each subunit is a 25 Da protein consisting of 224 residues bound together. The secondary structure is formed of one <scene name='71/719862/Helix/1'>α-helix</scene> and two antiparallel <scene name='71/719862/Sheet/1'>β-sheets</scene> <ref>[http://www.uniprot.org/uniprot/P02741 UniProtKB - P02741 (CRP_HUMAN)]</ref>. The predominant structure is β-sheet <ref>PMID: 1382589</ref> but short helical regions can be noticed for the residues 43 and 185 <ref name="kumar"/>. The residues Glu197 and Lys123 of CRP form an intermolecular ion pair <ref name="thompson">PMID: 10368284</ref>.
 The diameter of the CRP pentamer is 102 Å, the inner pore diameter is 30 Å and the diameter of a subunit is 36 Å <ref name="agrawal">PMID: 19799114 </ref>.