Flexibility of an antibody binding site measured with photon echo spectroscopy

被引:39
作者
Jimenez, R
Case, DA
Romesberg, FE
机构
[1] Scripps Res Inst, Dept Chem, La Jolla, CA 92037 USA
[2] Scripps Res Inst, Dept Mol Biol, La Jolla, CA 92037 USA
关键词
D O I
10.1021/jp013110g
中图分类号
O64 [物理化学(理论化学)、化学物理学];
学科分类号
070304 ; 081704 ;
摘要
The lock-and-key and induced fit models of antigen binding by antibodies are topics of considerable importance to immunology and protein biochemistry in general. These models ascribe different degrees of flexibility to the antibody combining site and may therefore be distinguished by measuring the response of the protein to the force exerted by charge redistribution and structural reorganization of an optically excited antigen. Spectroscopic characterization of the magnitude and time scale of this protein reorganization is therefore a basis for comparing the flexibility of different antibodies. This approach is used to study a panel of antibodies elicited to the chromophoric antigen 8-methoxypyrene-1,3,6,trisulfonic acid. The reorganization energies of the chromophore-antibody complexes are determined and are found to be distributed over a wide range. Three pulse photon echo peak shift spectroscopy is used to measure the time scales of the reorganization process in one complex. The antibody motions occur on time scales ranging from 75 femtoseconds to 67 picoseconds. Structural origins of the observed protein motions are discussed.
引用
收藏
页码:1090 / 1103
页数:14
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