How does sucrose stabilize the native state of globular proteins?

被引：33

作者：

Graziano, Giuseppe ^{[1
]}

机构：

[1] Univ Sannio, Dipartimento Sci Biol & Ambientali, I-82100 Benevento, Italy

来源：

INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES | 2012年 / 50卷 / 01期

关键词：

Sucrose; Protein conformational stability; Solvent-excluded volume effect; Work of cavity creation; SCALED-PARTICLE THEORY; CAVITY SIZE DISTRIBUTION; COMPATIBLE OSMOLYTE; MOLECULAR-DYNAMICS; THERMAL-STABILITY; INTERNAL DYNAMICS; EXCLUDED-VOLUME; RIBONUCLEASE-A; MIXED-SOLVENTS; FREE-ENERGY;

D O I：

10.1016/j.ijbiomac.2011.10.025

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

It is well known that sucrose stabilizes the native state of globular proteins against both chemical denaturants and temperature. A largely accepted explanation of sucrose-induced stabilization is not yet emerged. It is shown that the same theoretical approach able to rationalize the occurrence of cold denaturation, the contrasting role of GdmCl and Gdm(2)SO(4), and the TMAO counteraction of urea denaturing activity [PCCP 12 (2010) 14245; PCCP 13 (2011) 12008; PCCP 13 (2011) 17689] works well also in the case of sucrose. The solvent-excluded volume effect plays the fundamental role because sucrose addition to water causes a marked increase in volume packing density due to the large size of sucrose molecules, that act as crowding agents. (C) 2011 Elsevier B.V. All rights reserved.

引用

页码：230 / 235

页数：6

共 56 条

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