PROBING PROTEIN-STRUCTURE BY SOLVENT PERTURBATION OF NUCLEAR-MAGNETIC-RESONANCE SPECTRA - NUCLEAR-MAGNETIC-RESONANCE SPECTRAL EDITING AND TOPOLOGICAL MAPPING IN PROTEINS BY PARAMAGNETIC RELAXATION FILTERING

被引:67
作者
ESPOSITO, G
LESK, AM
MOLINARI, H
MOTTA, A
NICCOLAI, N
PASTORE, A
机构
[1] UNIV CAMBRIDGE, SCH CLIN, MRC CTR, DEPT HAEMATOL, CAMBRIDGE CB2 2QH, ENGLAND
[2] DIPARTIMENTO CHIM ORGAN & IND, I-20133 MILAN, ITALY
[3] CNR, IST CHIM MOLEC INTERESSE BIOL, I-80072 ARCO, ITALY
[4] UNIV LE SCOTTE, CTR DIDATTICO, DIPARTIMENTO BIOL MOLEC, I-53100 SIENNA, ITALY
关键词
TEMPOL; NMR; ESR; PROTEIN SURFACE;
D O I
10.1016/0022-2836(92)90551-T
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Soluble spin labels, which "bleach" the surface proton resonances of a protein to n.m.r. measurements, can provide useful information about protein conformation and dynamics. The use of the soluble nitroxide, TEMPOL, has been explored to show the correlation of the paramagnetic perturbations of protein two-dimensional n.m.r. data with proton exposure to the free radical in hen egg-white lysozyme. The results demonstrate that the nitroxide approaches the protein randomly, and that the extent of the observed paramagnetic effects reflects the native folding pattern of the protein. A correlation of spectral simplification with the known tertiary structure establishes the feasibility of new strategies for topological mapping of surface and buried protons of the protein. Application to the elucidation of protein structure and to the study of dynamical processes is discussed. © 1992.
引用
收藏
页码:659 / 670
页数:12
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