Format

Send to

Choose Destination
Protein Sci. 1996 Jul;5(7):1406-20.

Experimentally observed conformation-dependent geometry and hidden strain in proteins.

Author information

1
Section of Biochemistry, Molecular and Cell Biology, Cornell University, Ithaca, New York 14853, USA. pak4@cornell.edu

Abstract

A database has been compiled documenting the peptide conformations and geometries from 70 diverse proteins refined at 1.75 A or better. Analysis of the well-ordered residues within the database shows phi, psi-distributions that have more fine structure than is generally observed. Also, clear evidence is presented that the peptide covalent geometry depends on conformation, with the interpeptide N-C alpha-C bond angle varying by nearly +/-5 degrees from its standard value. The observed deviations from standard peptide geometry are greatest near the edges of well-populated regions, consistent with strain occurring in these conformations. Minimization of such hidden strain could be an important factor in thermostability of proteins. These empirical data describing how equilibrium peptide geometry varies as a function of conformation confirm and extend quantum mechanics calculations, and have predictive value that will aid both theoretical and experimental analyses of protein structure.

PMID:
8819173
PMCID:
PMC2143451
DOI:
10.1002/pro.5560050719
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for Wiley Icon for PubMed Central
Loading ...
Support Center