Interactions between Membranes and “Metaphilic” Polypeptide Architectures with Diverse Side-Chain Populations

Volume: 11, Issue: 3, Pages: 2858 - 2871
Published: Mar 17, 2017
Abstract
At physiological conditions, most proteins or peptides can fold into relatively stable structures that present on their molecular surfaces specific chemical patterns partially smeared out by thermal fluctuations. These nanoscopically defined patterns of charge, hydrogen bonding, and/or hydrophobicity, along with their elasticity and shape stability (folded proteins have Young’s moduli of ∼1 × 108 Pa), largely determine and limit the interactions...
Paper Details
Title
Interactions between Membranes and “Metaphilic” Polypeptide Architectures with Diverse Side-Chain Populations
Published Date
Mar 17, 2017
Journal
Volume
11
Issue
3
Pages
2858 - 2871
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