## Abstract Water proton 1/T~1~ nuclear magnetic relaxation dispersion (NMRD) profiles were measured for a water‐soluble gadolinium(III) texaphyrin (Gd‐tex) complex as a function of temperature and in the presence and absence of 5% human serum albumin (HSA). Upon dissolving the complex in water (0.
Nuclear magnetic relaxation dispersion study of the dynamics in solid homopolypeptides
✍ Scribed by Yanina Goddard; Jean-Pierre Korb; Robert G. Bryant
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 2007
- Tongue
- English
- Weight
- 251 KB
- Volume
- 86
- Category
- Article
- ISSN
- 0006-3525
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✦ Synopsis
Abstract
The ^1^H nuclear magnetic relaxation dispersion profiles were measured from 10 kHz to 30 MHz as a function of temperature for polyglycine, polyalanine, polyvaline, and polyphenylalanine to examine the contributions of different side chain motions to the polypeptide proton relaxation rate constants. The spin‐fracton theory for ^1^H relaxation is modified to account for high frequency motions of side chains that are dynamically connected to the linear polymer backbone. The ^1^H relaxation is dominated by propagation of rare disturbances along the backbone of the polymer. The side‐chain dynamics cause an off‐set in the field dependence of the ^1^H spin‐lattice relaxation rate constants which obey a power law in the Larmor frequency in the limit of low and high magnetic field strength. © 2007 Wiley Periodicals, Inc. Biopolymers 86: 148–154, 2007.
This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at [email protected]
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