ELECTROSTATIC INTERACTIONS IN HEMOGLOBIN FROM LIGHT-SCATTERING EXPERIMENTS

被引：14

作者：

LUNELLI, L ^{[1
]}

BUCCI, E ^{[1
]}

BALDINI, G ^{[1
]}

机构：

[1] UNIV MARYLAND,DEPT BIOCHEM,BALTIMORE,MD 21201

来源：

PHYSICAL REVIEW LETTERS | 1993年 / 70卷 / 04期

关键词：

D O I：

10.1103/PhysRevLett.70.513

中图分类号：

O4 [物理学];

学科分类号：

0702 ;

摘要：

Light scattering experiments on solutions of bovine CO-hemoglobin have revealed that a substantial component of the interactions responsible for the protein stability versus tetramer-to-dimer dissociation is due to electrostatic effects. Their magnitude has been estimated to reach congruent-to 4 kcal/mole (congruent-to 0.15 eV) at pH = 5 compared with the nonelectrostatic term which is of the order of 7 kcal/mole (congruent-to 0.3 eV).

引用

页码：513 / 516

页数：4

共 21 条

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