title: Extent of hydrogen-bond protection in folded proteins: a constraint on packing architectures.
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.
authors.affiliation: Institute for Biophysical Dynamics, The University of Chicago, 920 East 58th Street, Chicago, IL 60637, USA. ariel@uchicago.edu
authors.forename: Ariel
authors.initials: A
authors.lastname: Fernández
authors.forename: R Stephen
authors.initials: RS
authors.lastname: Berry
mesh_terms: D020816:Amino Acid Motifs; D019992:Databases as Topic; D006860:Hydrogen Bonding; D008958:Models, Molecular; D015233:Models, Statistical; D011487:Protein Conformation; D017510:Protein Folding; D014867:Water / Q000737:chemistry*
chemical_list: D014867:Water