Functional SAXS study of haemocyanin dioxygen-carrier protein

被引：4

作者：

Beltramini, M

Borghi, E

DiMuro, P

LaMonaca, A

Salvato, B

Santini, C

机构：

[1] UNIV PADUA,DIPARTIMENTO BIOL,I-35100 PADUA,ITALY

[2] CNR,CTR BIOCHIM & FISIOL MET PROT,I-35100 PADUA,ITALY

[3] UNIV ROMA LA SAPIENZA,DIPARTIMENTO CHIM,I-00185 ROME,ITALY

[4] IST NAZL FIS NUCL,LAB NAZL FRASCATI,I-00044 FRASCATI,ITALY

来源：

JOURNAL OF MOLECULAR STRUCTURE | 1996年 / 383卷 / 1-3期

关键词：

small angle X-ray scattering; haemocyanins; conformational rearrangement;

D O I：

10.1016/S0022-2860(96)09292-7

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070304 ; 081704 ;

摘要：

The effects of conformational rearrangements on dioxygen binding to molluscan haemocyanins have been investigated by small-angle X-ray scattering (SAXS), The SAXS patterns of the oxygenated and deoxygenated forms of Octopus vulgaris haemocyanin are significantly different; whereas the patterns of the two forms of Rapana thomasiana haemocyanin are almost superimposable. A program has been developed, based on the differences in molecular dimensions, in order to simulate the effects observed in the investigation.

引用

页码：237 / 240

页数：4