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The biological functions of low‐frequency vibrations (phonons). VI. A possible dynamic mechanism of allosteric transition in antibody molecules
Author(s) -
Chou KuoChen
Publication year - 1987
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.360260209
Subject(s) - chemistry , allosteric regulation , molecule , low frequency , raman spectroscopy , function (biology) , mechanism (biology) , chemical physics , signal (programming language) , spectral line , resonance (particle physics) , biophysics , molecular physics , stereochemistry , atomic physics , physics , quantum mechanics , biochemistry , receptor , organic chemistry , astronomy , evolutionary biology , computer science , biology , programming language
By means of the quasi‐continuity theory developed recently [Chou, K.‐C. (1983) Biochem. J. 209 , 573–580; Chou, K.‐C. (1984) Biochem. J. 221 , 27–31; Chou, K.‐C. (1985) Biophys. J. 48 , 289–297], the low‐frequency breathing motions of the β‐barrels in the 12 domains of an IgG antibody molecule have been calculated. The results are in very good agreement with the observed low‐frequency peaks in the Raman spectra. Based on this, the resonant couplings among the domains located at its different regions are discussed. It turns out that some very interesting functions of antibody molecules, such as the “chelate effect” and “trigger effect” whose dynamic principle has been so far unknown, can be clearly elucidated in terms of a fundamental natural law; i.e., it is through the channel of low‐frequency resonance that the “signal” (or energy) in an antibody is transmitted from one location to the other, so as to be able to induce the relevant conformational change required for operating those important biological functions. The physical picture illustrated here once again provides us with a classic example that structure and function in nature are highly harmonized.