Protein thermal stabilization in aqueous solutions of osmolytes

被引：16

作者：

Bruzdziak, Piotr ^{[1
]}

Panuszko, Aneta ^{[1
]}

Jourdan, Muriel ^{[2
]}

Stangret, Janusz ^{[1
]}

机构：

[1] Gdansk Univ Technol, Fac Chem, Dept Phys Chem, Gdansk, Poland

[2] Univ Grenoble, ICMG FR2607, CNRS UMR5250, Dept Chim Mol, F-570 Grenoble 9, France

来源：

ACTA BIOCHIMICA POLONICA | 2016年 / 63卷 / 01期

关键词：

water structure; protein stability; circular dichroism; FT-IR spectroscopy; DFT calculations; TRIMETHYLAMINE-N-OXIDE; MOLECULAR-MECHANISM; GLYCINE BETAINE; WATER; UREA; DENATURATION; STABILITY; HYDRATION; SOLUTES; MODEL;

D O I：

10.18388/abp.2014_950

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：

Proteins' thermal stabilization is a significant problem in various biomedical, biotechnological, and technological applications. We investigated thermal stability of hen egg white lysozyme in aqueous solutions of the following stabilizing osmolytes: Glycine (GLY), N-methylglycine (NMG), N,N-dimethylglycine (DMG), N, N, N-trimethylglycine (TMG), and trimethyl-N-oxide (TMAO). Results of CD-UV spectroscopic investigation were compared with FTIR hydration studies' results. Selected osmolytes increased lysozyme's thermal stability in the following order: Gly>NMG>TMAO approximate to DMG> TMG. Theoretical calculations (DFT) showed clearly that osmolytes' amino group protons and water molecules interacting with them played a distinctive role in protein thermal stabilization. The results brought us a step closer to the exact mechanism of protein stabilization by osmolytes.

引用

页码：65 / 70

页数：6

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