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1bsq

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{{STRUCTURE_1bsq| PDB=1bsq | SCENE= }}
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'''STRUCTURAL AND FUNCTIONAL CONSEQUENCES OF POINT MUTATIONS OF VARIANTS A AND B OF BOVINE BETA-LACTOGLOBULIN'''
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===STRUCTURAL AND FUNCTIONAL CONSEQUENCES OF POINT MUTATIONS OF VARIANTS A AND B OF BOVINE BETA-LACTOGLOBULIN===
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==Overview==
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The structure of the trigonal crystal form of bovine beta-lactoglobulin variant B at pH 7.1 has been determined by X-ray diffraction methods at a resolution of 2.22 A and refined to values for R and Rfree of 0.239 and 0.286, respectively. By comparison with the structure of the trigonal crystal form of bovine beta-lactoglobulin variant A at pH 7.1, which was determined previously [Qin BY et al., 1998, Biochemistry 37:14014-14023], the structural consequences of the sequence differences D64G and V118A of variants A and B, respectively, have been investigated. Only minor differences in the core calyx structure occur. In the vicinity of the mutation site D64G on loop CD (residues 61-67), there are small changes in main-chain conformation, whereas the substitution V118A on beta-strand H is unaccompanied by changes in the surrounding structure, thereby creating a void volume and weakened hydrophobic interactions with a consequent loss of thermal stability relative to variant A. A conformational difference is found for the loop EF, implicated in the pH-dependent conformational change known as the Tanford transition, but it is not clear whether this reflects differences intrinsic to the variants in solution or differences in crystallization.
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(as it appears on PubMed at http://www.pubmed.gov), where 10210185 is the PubMed ID number.
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{{ABSTRACT_PUBMED_10210185}}
==About this Structure==
==About this Structure==
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[[Category: Hydrophobic]]
[[Category: Hydrophobic]]
[[Category: Point mutation]]
[[Category: Point mutation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:54:44 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 19:39:56 2008''

Revision as of 16:39, 30 June 2008

Image:1bsq.png

Template:STRUCTURE 1bsq

STRUCTURAL AND FUNCTIONAL CONSEQUENCES OF POINT MUTATIONS OF VARIANTS A AND B OF BOVINE BETA-LACTOGLOBULIN

Template:ABSTRACT PUBMED 10210185

About this Structure

1BSQ is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

Reference

Functional implications of structural differences between variants A and B of bovine beta-lactoglobulin., Qin BY, Bewley MC, Creamer LK, Baker EN, Jameson GB, Protein Sci. 1999 Jan;8(1):75-83. PMID:10210185

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