Role of the N‐terminus in the structure and stability of chicken annexin V

FEBS Letters

Arboledas, David¹  Turnay, Javier¹  Lizarbe, Mª Antonia¹  Olmo, Nieves¹ 

[1] Departamento de Bioquı́mica y Biologı́a Molecular, Facultad de Ciencias Quı́micas, Universidad Complutense, 28040-Madrid, Spain

关键词: Annexin V;    Calcium binding;    Circular dichroism spectroscopy;    Fluorescence emission spectroscopy;    CD;    circular dichroism;    EGTA;    ethylene glycol-bis(β-aminoethyl ether) N;    N;    N′;    N′-tetraacetic acid;    IPTG;    isopropyl-β-d-thiogalactopyranoside;    PAGE;    polyacrylamide gel electrophoresis;    PS;    phosphatidylserine;    SDS;    sodium dodecyl sulfate;    UV;    ultraviolet;   

DOI  :  10.1016/S0014-5793(97)01207-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown