PMID: 37429Sep 1, 1976

NMR spin-echo study of behaviour dynamics of serum albumin macromolecules in aqueous solutions as a function of pH and ionic strength

Molekuliarnaia biologiia
S I AksenovV N Vitvitskiĭ


Alteration of the intermolecular interaction in aqueous solution of human serum albumin (SA) as a result of the increase of ionic strength and pH values brings about the slowing-down of the spin-echo decay curve for protein protons (several times at high SA concentrations). A specific effect of alkaline pH was observed, i.e. the slowing-down of quick component of the spin-echo decay curve. This result taken together with the data on complex spin-echo decay curve, correlation times of protons of different regions is SA and compared with SA isotope exchange data can be explained as a result of the polypeptide chain conformation mobility with frequencies more 10(4) c.p.s. This effect is observed in regions occupying about one half of the SA macromolecule volume.

Related Concepts

Serum Albumin Measurement
In Vivo NMR Spectroscopy
Albumin Human, USP
Human Serum Albumin [EPC]
Protein Conformation
Plasma Albumin
Aqueous solution

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