A molecular theory of relaxation and magnetization transfer: application to cross-linked BSA, a model for tissue.

Abstract:

:Homogeneous soft tissue, as regards its magnetic relaxation properties, is well-modeled by solutions of cross-linked protein (see Koenig and Brown, Prog. NMR Spectr. 22, 487 (1991)). Interactions at the solute-solvent interface alter the hydrodynamics of solvent water, and also couple the solute and solvent proton Zeeman energy reservoirs, giving hydrodynamic and cross-relaxation contributions to water proton relaxation that respond differently to deuteration of solvent. We report measurements of the magnetic field dependence of 1/T1 of water protons in cross-linked bovine serum albumin (BSA), for partially deuterated solvent and, in order to separate these two contributions, of 1/T1 of deuterons. The major experimental finding is that, in addition to recently identified water-binding sites on protein (covering approximately 0.2% of the surface) with water lifetimes of about 1 microsecond, there is another group of sites with lifetimes of about 23 ns, covering approximately 2% of the surface, which are evident in both proton and deuteron data. In addition, we have formulated a theory of interfacial proton-proton magnetic interactions which--with these four parameters, plus two that quantify the protein-water coupling at each site--can account for all the proton and deuteron data, in both native and cross-linked BSA.

journal_name

Magn Reson Med

authors

Koenig SH,Brown RD 3rd

doi

10.1002/mrm.1910300606

subject

Has Abstract

pub_date

1993-12-01 00:00:00

pages

685-95

issue

6

eissn

0740-3194

issn

1522-2594

journal_volume

30

pub_type

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