NMR relaxation investigation of water mobility in aqueous bovine serum albumin solutions.

L Grösch, F Noack
Author Information

Abstract

T1 and T2 dispersion measurements of proton spin relaxation on aqueous solutions of bovine serum albumin as a function of both protein concentration and temperature, covering Larmor frequencies from 3 kHz to 75 MHz, will be presented as a most conclusive test for a three-phase fast-exchange relaxation model. By means of a computer curve fitting of this model to the experimental data, we were able to separate 3 distinct water environments and, in addition, the rotational tumbling of the bovine serum albumin molecules.

MeSH Term

Hydrogen Bonding
Magnetic Resonance Spectroscopy
Mathematics
Protein Binding
Protein Conformation
Serum Albumin, Bovine
Water

Chemicals

Water
Serum Albumin, Bovine

Word Cloud

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