On the satisfaction of backbone-carbonyl lone pairs of electrons in protein structures.

ABSTRACT: Protein structures are stabilized by a variety of noncovalent interactions (NCIs), including the hydrophobic effect, hydrogen bonds, electrostatic forces and van der Waals' interactions. Our knowledge of the contributions of NCIs, and the interplay between them remains incomplete. This has implications for computational modeling of NCIs, and our ability to understand and predict protein structure, stability, and function. One consideration is the satisfaction of the full potential for NCIs made by backbone atoms. Most commonly, backbone-carbonyl oxygen atoms located within α-helices and β-sheets are depicted as making a single hydrogen bond. However, there are two lone pairs of electrons to be satisfied for each of these atoms. To explore this, we used operational geometric definitions to

SUBMITTER: Bartlett GJ 

PROVIDER: S-EPMC4941217 | biostudies-literature | 2016 Apr

REPOSITORIES: biostudies-literature