User:Manon Raiffort/Sandbox: Difference between revisions

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=== A3 domain ===

A3 domain is a domain of 20kDa between the residues 920 to 1111 of the von willebrand factor.

It has a dinucleotide-binding fold. This is a structure in which a central β sheet is encompassed by 7 α-helix (named α1 to α7) connected by loops. The β sheet is composed by 6 strands (named respectively β1 to β6) and are all parallel except the β3 which is on the sheet’s edge.

In this domain, two cysteine residues (923 and 1109) put the N-terminal and C-terminal region together by a disulfide bond.

The A3 domain is composed of negative charged and this allows the interaction with the collagen which has positive charged residues on it.

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

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 === A3 domain ===
 A3 domain is a domain of 20kDa between the residues 920 to 1111 of the von willebrand factor.
 It has a dinucleotide-binding fold. This is a structure in which a central β sheet is encompassed by 7 α-helix (named α1 to α7) connected by loops. The β sheet is composed by 6 strands (named respectively β1 to β6) and are all parallel except the β3 which is on the sheet’s edge.
 In this domain, two cysteine residues (923 and 1109) put the N-terminal and C-terminal region together by a disulfide bond.
 The A3 domain is composed of negative charged and this allows the interaction with the collagen which has positive charged residues on it.
 This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.