PMID: 3214182Dec 1, 1988Paper

Oxygen-17 and deuterium nuclear magnetic relaxation studies of lysozyme hydration in solution: field dispersion, concentration, pH/pD, and protein activity dependences

Archives of Biochemistry and Biophysics
L T Kakalis, I C Baianu

Abstract

A comparison of 17O and 2H NMR relaxation rates of water in lysozyme solutions as a function of concentration, pH/pD, and magnetic field suggests that only 17O monitors directly the hydration of lysozyme in solution. NMR measurements are for the first time extended to 11.75 T. Lysozyme hydration data are analyzed in terms of an anisotropic, dual-motion model with fast exchange of water between the "bound" and "free" states. The analysis yields 180 mol "bound" water/mol lysozyme and two correlation times of 7.4 ns ("slow") and 29 ps ("fast") for the bound water population at 27 degrees C and pH 5.1, in the absence of salt, assuming anisotropic motions of water with an order parameter value for bound water of 0.12. Under these conditions, the value of the slow correlation time of bound water (7.4 ns) is consistent with the value of 8 ns obtained by frequency-domain fluorescence techniques for the correlation time associated with the lysozyme tumbling motion in solutions without salt. In the presence of 0.1 M NaCl the hydration number increases to 290 mol/mol lysozyme at pD 4.5 and 21 degrees C. The associated correlation times at 21 degrees C in the presence of 0.1 M NaCl are 4.7 ns and 15.5 ps, respectively. The value of the slo...Continue Reading

References

Oct 3, 1978·Biochemistry·S H KoenigG S Jacob
Oct 1, 1977·Archives of Biochemistry and Biophysics·E Hsi, R G Bryant
Jul 1, 1975·Proceedings of the National Academy of Sciences of the United States of America·S H KoenigM Shporer
May 1, 1976·Biopolymers·G E Ellis, K J Packer
Apr 1, 1986·Biophysical Journal·H PeemoellerA R Sharp
May 15, 1986·Archives of Biochemistry and Biophysics·T S LioutasM P Steinberg
Oct 1, 1986·Biochemical Society Transactions·E GrattonG Marriott
Mar 30, 1973·Annals of the New York Academy of Sciences·H J Berendsen, H T Edzes
Jan 1, 1974·Advances in Protein Chemistry·I D Kuntz, W Kauzmann
Sep 1, 1973·Archives of Biochemistry and Biophysics·H Saitô, I C Smith
May 1, 1972·Archives of Biochemistry and Biophysics·S N Timasheff, J A Rupley
Oct 12, 1972·The Journal of Physical Chemistry·S C Harvey, P Hoekstra
Feb 1, 1967·Journal of Biochemistry·K Ogasahara, K Hamaguchi
Dec 7, 1982·Biochemistry·T Arakawa, S N Timasheff
Oct 1, 1952·Proceedings of the National Academy of Sciences of the United States of America·J G Kirkwood, J B Shumaker

❮ Previous
Next ❯

Citations

Dec 1, 1994·Biopolymers·J P RenouP Gatellier
Jul 7, 1999·Biochimica Et Biophysica Acta·E GoormaghtighJ M Ruysschaert
Jan 1, 1996·Magnetic Resonance in Medicine : Official Journal of the Society of Magnetic Resonance in Medicine·E Liepinsh, G Otting
Mar 6, 2003·Journal of Agricultural and Food Chemistry·Elena VittadiniPavinee Chinachoti
Jan 12, 2010·Spectrochimica Acta. Part A, Molecular and Biomolecular Spectroscopy·Matteus LindgrenPer-Olof Westlund

❮ Previous
Next ❯

Related Concepts

Related Feeds

Bacterial Cell Wall Structure (ASM)

Bacterial cell walls are made of peptidoglycan (also called murein), which is made from polysaccharide chains cross-linked by unusual peptides containing D-amino acids. Here is the latest research on bacterial cell wall structures.

Bacterial Cell Wall Structure

Bacterial cell walls are made of peptidoglycan (also called murein), which is made from polysaccharide chains cross-linked by unusual peptides containing D-amino acids. Here is the latest research on bacterial cell wall structures.