The radius of gyration of L-arabinose-binding protein decreases upon binding of ligand.
نویسندگان
چکیده
منابع مشابه
Relating protein dynamics to the thermodynamics of ligand binding in arabinose binding protein
Introduction The interactions of proteins with small molecule ligands are of central importance to much of biology. The ability to predict and manipulate such interactions will open a number of future avenues in research, biotechnology and therapeutics. In particular, an understanding of the molecular basis of protein-small molecule interactions is crucial to attempts to design novel drug techn...
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Structural study of hinge bending in L-arabinose-binding protein.
The L-arabinose-binding protein of Escherichia coli is a periplasmic component of the bacterial L-arabinose transport system. The three-dimensional structure of the molecule has been determined by x-ray diffraction and shown to have two globular domains and a connecting hinge. Theoretical study of the flexibility of the hinge using computer simulation showed that the hinge is quite permissive i...
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چکیده ندارد.
15 صفحه اولL-arabinose binding protein from Escherichia coli B-r.
A protein which is capable of binding l-arabinose-1-(14)C has been isolated from l-arabinose-induced cultures of Escherichia coli B/r. Analysis for this l-arabinose-binding protein (ABP) in a number of l-arabinose-negative mutants suggests that the ABP is not coded for by any of the known genetic units of the l-arabinose complex yet is under the control of the regulator gene araC. The ABP has b...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1981
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)43030-x