Conformational Studies of the C-Terminal 16-Amino-Acid-Residue Fragment of the B3 Domain of the Immunoglobulin Binding Protein G fromStreptococcus

Biopolymers- United States

doi 10.1002/bip.21080

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Date

January 1, 2009

Authors

Agnieszka Skwierawska

Stanisław Ołdziej

Adam Liwo

Harold A. Scheraga

Publisher

Wiley

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Conformational Studies of the C-Terminal 16-Amino-Acid-Residue Fragment of the B3 Domain of the Immunoglobulin Binding Protein G fromStreptococcus

Biopolymers- United States

Full Text

Abstract

Categories

Date

Authors

Publisher

Related search

Conformational Studies of the Α-Helical 28-43 Fragment of the B3 Domain of the Immunoglobulin Binding Protein G fromStreptococcus

Mechanism of Formation of the C-Terminal Β-Hairpin of the B3 Domain of the Immunoglobulin Binding Protein G fromStreptococcus. III. Dynamics of Long-Range Hydrophobic Interactions

Mechanism of Formation of the C-Terminal Β-Hairpin of the B3 Domain of the Immunoglobulin Binding Protein G fromStreptococcus. I. Importance of Hydrophobic Interactions in Stabilization of Β-Hairpin Structure

Mechanism of Formation of the C-Terminal Β-Hairpin of the B3 Domain of the Immunoglobulin-Binding Protein G From Streptococcus. IV. Implication for the Mechanism of Folding of the Parent Protein

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