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FEBS Lett ; 416(2): 217-20, 1997 Oct 20.
Article in English | MEDLINE | ID: mdl-9369218

ABSTRACT

The role of the short N-terminal region of chicken annexin V in the maintenance of the protein structure and its influence in the conformation of the calcium binding regions was analyzed. The N-terminal domain is not essential for protein folding, wild-type and dnt-annexin V showing almost identical secondary structures. However, the partial truncation of the N-terminus significantly decreases the melting temperature of the protein and induces the partial exposure of Trp187 which is normally located in a hydrophobic pocket of the calcium binding region of domain 3 of annexin V in the Ca2+-free form.


Subject(s)
Annexin A5/chemistry , Protein Conformation , Animals , Annexin A5/biosynthesis , Chickens , Circular Dichroism , Drug Stability , Hot Temperature , Mutagenesis, Site-Directed , Protein Denaturation , Recombinant Proteins/biosynthesis , Recombinant Proteins/chemistry , Sequence Deletion , Spectrometry, Fluorescence , Thermodynamics
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