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Updated: Aug 10, 2026

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues
Published on: July 14, 2015
Extent of hydrogen-bond protection in folded proteins: a constraint on packing architectures
Ariel Fernández1, R Stephen Berry
1Institute for Biophysical Dynamics, The University of Chicago, 920 East 58th Street, Chicago, IL 60637, USA. ariel@uchicago.edu
Abstract:
Progressive structuring and ultimately exclusion of water by hydrophobes surrounding backbone hydrogen bonds turn the latter into guiding factors of protein folding. Here we demonstrate that an arrangement of five hydrophobes yields an optimal hydrogen-bond stabilization. This motif is shown to be nearly ubiquitous in native folds.
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