Using NMR-detected hydrogen-deuterium exchange to quantify protein stability in cosolutes,under crowded conditions in vitro and in cells  

作　　者：I-Te Chu Gary J.Pielak 

机构地区：[1]Department of Chemistry,University of North Carolina at Chapel Hill(UNC-CH),Chapel Hill,NC,27599-3290,United States [2]Department of Biochemistry and Biophysics,UNC-CH,Chapel Hill,NC,27599-3290,United States [3]Lineberger Cancer Center,UNC-CH,Chapel Hill,NC,27599-3290,United States [4]Integrative Program for Biological and Genome Sciences,UNC-CH,Chapel Hill,NC,27599-7100,United States

出　　处：《Magnetic Resonance Letters》2023年第4期319-326,共8页磁共振快报（英文）

摘　　要：We review the use of nuclear magnetic resonance(NMR)spectroscopy to assess the exchange of amide protons for deuterons(HDX)in efforts to understand how high concentration of cosolutes,especially macromolecules,affect the equilibrium thermodynamics of protein stability.HDX NMR is the only method that can routinely provide such data at the level of individual amino acids.We begin by discussing the properties of the protein systems required to yield equilibrium thermodynamic data and then review publications using osmolytes,sugars,denaturants,synthetic polymers,proteins,cytoplasm and in cells.

关 键 词：Amide proton exchange Cosolutes Equilibrium thermodynamics Macromolecular CROWDING OSMOLYTES Protein stability 

分 类 号：O62[理学—有机化学]