FEBS Letters | |
Role of the N‐terminus in the structure and stability of chicken annexin V | |
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
【 预 览 】
Files | Size | Format | View |
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RO201912020305092ZK.pdf | 695KB | download |