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Assesment of protein reorientational diffusion in solution by 13 C off‐resonance rotating frame spin–lattice relaxation: Effect of polydispersity
Author(s) -
Morgan Courtney F.,
Schiliech Thomas,
Caines G. Herbert
Publication year - 1990
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.360290305
Subject(s) - chemistry , rotational diffusion , dispersity , lysozyme , isotropy , formalism (music) , bovine serum albumin , population , nuclear magnetic resonance , chemical physics , chromatography , polymer chemistry , organic chemistry , molecule , biochemistry , optics , physics , art , musical , demography , sociology , visual arts
The 13 C off‐resonance rotating frame spin‐lattice relaxation technique is applicable to the study of protein rotational diffusion behavior in both model in vitro and in vivo systems. The original formalism of James and co‐workers [(1978) J. Am. Chem. Soc. 100 , 3590–3594] was constrained by the assumption of random isotropic reorientational motion of a monodisperse protein population. Here we extend the formalism to include polydispersity. Application is made to the alkaline pH induced association of lysozyme, lysozyme–bovine serum albumin mixtures, and to the phase separation of lysozyme salt–water mixtures induced by low temperature.