PMID: 560299May 16, 1977

The determination of molecular-motion parameters from proton-relaxation-enhancement measurements in a number of Gd(III) - antibody-fragment complexes. A comparative study

European Journal of Biochemistry
D R BurtonS Wain-Hobson


Longitudinal and transverse proton relaxation rates for water in the hydration spheres of Gd(III) bound to the non-immune rabbit IgG fragments Fc (C-terminal half of heavy-chain dimer), pFc' (C-terminal quarter of heavy-chain dimer) and Fab (N-terminal half of heavy and light chain) have been measured at a number of frequencies and temperatures using pulsed nuclear magnetic resonance spectrometry. For the fragments Fc and pFc', a full computer analysis showed that the results could be fitted by parameters of similar magnitude to those found previously for IgG. In contrast to the results for the other complexes the Fab -Gd(III) complex showed no slow exchange contribution to the relaxation rates. Under these circumstances it was found possible to obtain an accurate value for the hydration number (q) from measurements of the longitudinal and transverse relaxation rates at a chosen frequency such that the product of the nuclear Larmor frequency (omega1) and the correlation time for the dipolar relaxation processes (tauc) was approximately unity. Water-proton relaxation rates were also determined for the complex of Gd(III) with the Fv fragment of the mouse myeloma protein MOPC 315. A computer analysis of the results revealed a slow...Continue Reading


Jul 1, 1975·The Biochemical Journal·S K DowerC A Sunderland
Jan 1, 1975·Advances in Protein Chemistry·G Weber
Feb 1, 1973·Proceedings of the National Academy of Sciences of the United States of America·S H KoenigC F Brewer


Aug 1, 1989·Quarterly Reviews of Biophysics·A R Holzwarth
Jan 1, 1981·CRC Critical Reviews in Biochemistry·M Karplus, J A McCammon

Related Concepts

Binding Sites, Antibody
Computers, Digital
Antibody Fragments
Fab Immunoglobulins
Immunoglobulin Fc Fragments
In Vivo NMR Spectroscopy

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