Functional implications of structural differences between variants A and B of bovine β-lactoglobulin

The structure of the trigonal crystal form of bovine β-lactoglobulin variant B at pH 7.1 has been determined by X-ray diffraction methods at a resolution of 2.22 Å 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...

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Veröffentlicht in:	Protein science 1999-01, Vol.8 (1), p.75-83
Hauptverfasser:	QIN, BIN Y., BEWLEY, MARIA C., CREAMER, LAWRENCE K., BAKER, EDWARD N., JAMESON, GEOFFREY B.
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Substitution Animals bovine β‐lactoglobulin Cattle crystal structure Crystallography, X-Ray genetic variants Hydrogen-Ion Concentration hydrophobic stabilization Lactoglobulins - chemistry Models, Molecular Protein Conformation Protein Isoforms - chemistry
Online-Zugang:	Volltext
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