Repeating Aspartic Acid Residues Prefer Turn-like Conformations in the Unfolded State: Implications for Early Protein Folding

Volume: 125, Issue: 41, Pages: 11392 - 11407
Published: Oct 7, 2021
Abstract
Protein folding can be described as a motion of the polypeptide chain in a potential energy funnel, where the conformational manifold is narrowed as the chain traverses from a completely unfolded state until it reaches the folded (native) state. The initial folding stages set the tone for this process by substantially narrowing the manifold of accessible conformations. In an ideally unfolded state with no long-range stabilizing forces, local...
Paper Details
Title
Repeating Aspartic Acid Residues Prefer Turn-like Conformations in the Unfolded State: Implications for Early Protein Folding
Published Date
Oct 7, 2021
Volume
125
Issue
41
Pages
11392 - 11407
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