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Amide exchange shows calcium-induced conformational changes are transmitted to the dimer interface of S100

Authors :
Marlatt, Nicole M.
Shaw, Gary S.
Source :
Biochemistry. June 26, 2007, Vol. 46 Issue 25, p7478, 10 p.
Publication Year :
2007

Abstract

S100B is a calcium-binding protein, which binds calcium and also undergoes certain changes, exposing the hydrophobic surface residues. Such conformational changes help the protein to interact with various biological target molecules, also maintaining a balance between the amide exchange rates.

Details

Language :
English
ISSN :
00062960
Volume :
46
Issue :
25
Database :
Gale General OneFile
Journal :
Biochemistry
Publication Type :
Academic Journal
Accession number :
edsgcl.167547100