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A study of apo‐ and holo‐forms of horse liver alcohol dehydrogenase in solution by diffuse X‐ray scattering
Author(s) -
Yu. Pavlov M.,
Sinev M. A.,
Timchenko A. A.,
Ptitsyn O. B.
Publication year - 1986
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.360250803
Subject(s) - chemistry , scattering , alcohol dehydrogenase , crystallography , small angle x ray scattering , x ray , crystal (programming language) , dehydrogenase , enzyme , optics , physics , organic chemistry , programming language , computer science
Apo‐ and holo‐forms of horse liver alcohol dehydrogenase (LADH) in solution were studied by diffuse x‐ray scattering. Experimental scattering curves for apo‐ and holo‐forms coincide both with the curves calculated from the crystal structures of apo‐ and holo‐enzymes, and with each other. Thus the “sliding” of catalytical domains in LADH upon substrate binding, which has been shown by x‐ray analysis, cannot be detected by diffuse x‐ray scattering. Sensitivity of the scattering curves to the domain displacements of sliding and “locking” types has been investigated. It has been shown that the scattering curves of LADH are rather sensitive to the domain “unlocking.” However, these curves change only slightly upon sliding of domains, including the sliding of domains observed in LADH by x‐ray analysis.