期刊
JOURNAL OF PHYSICAL CHEMISTRY B
卷 114, 期 51, 页码 17062-17067出版社
AMER CHEMICAL SOC
DOI: 10.1021/jp108995k
关键词
-
资金
- Natural Sciences and Engineering Research Council (NSERC) of Canada
Protein aggregation is an important biophysical phenomenon, and it is technically challenging to quantify. Scattering studies in concentrated protein solutions are not in complete agreement over the existence of an equilibrium cluster phase. We use pulsed-field-gradient NMR spectroscopy to characterize diffusion in the long-time limit in concentrated lysozyme solutions and find strong evidence for the existence a an equilibrium phase that consists of both lysozyme monomers and clusters (aggregates). They indicate too that there is rapid exchange between monomer and aggregate on the NMR time scale, and that macroscopic measurables (e.g., the relaxation rate and the observed diffusion coefficient) reflect a weighted average of the two fractions. Our results are quantitatively compared, with no fit parameters, to simple theories of macromolecular crowding.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据