Document Detail


Empirical torsional potential functions from protein structure data. Phi- and psi-potentials for non-glycyl amino acid residues.
MedLine Citation:
PMID:  489256     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The torsional potential functions Vt(phi) and Vt(psi) around single bonds N--C alpha and C alpha--C, which can be used in conformational studies of oligopeptides, polypeptides and proteins, have been derived, using crystal structure data of 22 globular proteins, fitting the observed distribution in the (phi, psi)-plane with the value of Vtot(phi, psi), using the Boltzmann distribution. The averaged torsional potential functions, obtained from various amino acid residues in L-configuration, are Vt(phi) = 1.0 cos (phi + 60 degrees); Vt(psi) = 0.5 cos (psi + 60 degrees) - 1.0 cos (2 psi + 30 degrees) - 0.5 cos (3 psi + 30 degrees). The dipeptide energy maps Vtot(phi, psi) obtained using these functions, instead of the normally accepted torsional functions, were found to explain various observations, such as the absence of the left-handed alpha helix and the C7 conformation, and the relatively high density of points near the line psi = 0 degrees. These functions derived from observational data on protein structures, will, it is hoped, explain various previously unexplained facts in polypeptide conformation.
Authors:
A S Kolaskar; D Prashanth
Related Documents :
11806946 - C-deuterated alanine: a new label to study membrane protein structure using site-specif...
16001716 - Interaction of 1-dodecyl-azacycloheptan-2-one with mouse stratum corneum.
11714926 - Molecular design of mycoplasma hominis vaa adhesin.
16132146 - Study of the conformation of gamma-zeins in purified maize protein bodies by ftir and n...
9865606 - Transcription of the rat p53 gene is mediated by factor binding to two recognition moti...
24849606 - Increased c-telopeptide cross-linking of tendon type i collagen in fibromodulin-deficie...
Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  International journal of peptide and protein research     Volume:  14     ISSN:  0367-8377     ISO Abbreviation:  Int. J. Pept. Protein Res.     Publication Date:  1979 Aug 
Date Detail:
Created Date:  1979-12-20     Completed Date:  1979-12-20     Revised Date:  2000-12-18    
Medline Journal Info:
Nlm Unique ID:  0330420     Medline TA:  Int J Pept Protein Res     Country:  DENMARK    
Other Details:
Languages:  eng     Pagination:  88-98     Citation Subset:  IM    
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Crystallization
Peptide Fragments
Protein Conformation*
Chemical
Reg. No./Substance:
0/Peptide Fragments

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  Studies on peptides. LXXXI. Application of a new arginine derivative, NG-mesitylene-2-sulfonylargini...
Next Document:  Comparative temperature-stability properties of malate dehydrogenases from some thermophilic fungi.