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

Proteins: Structure, Function and Genetics- United States

doi 10.1002/prot.22304

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Date

June 1, 2009

Authors

Agnieszka Skwierawska

Publisher

Wiley

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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

Proteins: Structure, Function and Genetics- United States

Full Text

Abstract

Categories

Date

Authors

Publisher

Related search

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 From Streptococcus. IV. Implication for the Mechanism of Folding of the Parent Protein

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

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

Dynamics of Metastable Β-Hairpin Structures in the Folding Nucleus of Amyloid Β-Protein

Using Computational Modeling to Understand the Binding Mechanism of Designed Cyclic Β-Hairpin to MDM2

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Amyloid Β-Protein C-Terminal Fragments: Formation of Cylindrins and Β-Barrels

The Catalytic Mechanism of the Hairpin Ribozyme