NDLI: Structural and thermodynamic analysis of the binding of solvent at internal sites in T4 lysozyme.

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Structural and thermodynamic analysis of the binding of solvent at internal sites in T4 lysozyme.

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Structural and thermodynamic analysis of the binding of solvent at internal sites in T4 lysozyme.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Matthews, B. W. Xu, J. Baldwin, E. P. Quillin, M. L. Baase, W. A.
Description	Country affiliation: United States Author Affiliation: Xu J ( Institute of Molecular Biology, Howard Hughes Medical Institute and Department of Physics, University of Oregon, Eugene, Oregon 97403, USA.)
Abstract	To investigate the structural and thermodynamic basis of the binding of solvent at internal sites within proteins a number of mutations were constructed in T4 lysozyme. Some of these were designed to introduce new solvent-binding sites. Others were intended to displace solvent from preexisting sites. In one case Val-149 was replaced with alanine, serine, cysteine, threonine, isoleucine, and glycine. Crystallographic analysis shows that, with the exception of isoleucine, each of these substitutions results in the binding of solvent at a polar site that is sterically blocked in the wild-type enzyme. Mutations designed to perturb or displace a solvent molecule present in the native enzyme included the replacement of Thr-152 with alanine, serine, cysteine, valine, and isoleucine. Although the solvent molecule was moved in some cases by up to 1.7 A, in no case was it completely removed from the folded protein. The results suggest that hydrogen bonds from the protein to bound solvent are energy neutral. The binding of solvent to internal sites within proteins also appears to be energy neutral except insofar as the bound solvent may prevent a loss of energy due to potential hydrogen bonding groups that would otherwise be unsatisfied. The introduction of a solvent-binding site appears to require not only a cavity to accommodate the water molecule but also the presence of polar groups to help satisfy its hydrogen-bonding potential. It may be easier to design a site to accommodate two or more water molecules rather than one as the solvent molecules can then hydrogen-bond to each other. For similar reasons it is often difficult to design a point mutation that will displace a single solvent molecule from the core of a protein.
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science
Issue Number	5
Volume Number	10
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	2001-05-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Bacteriophage T4 Enzymology Muramidase Chemistry Metabolism Solvents Amino Acid Substitution Genetics Binding Sites Crystallography, X-ray Enzyme Stability Hydrogen Bonding Models, Molecular Point Mutation Protein Binding Protein Conformation Thermodynamics Research Support, U.s. Gov't, P.h.s. Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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