Home LiteratureArticle Details
PMID: 2386807 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

The sampling properties of some distance geometry algorithms applied to unconstrained polypeptide chains: a study of 1830 independently computed conformations.

Biopolymers ·Vol. 29 ·No. 12-13 ·1990-00-00 ·Pages 1565-85

Havel TF

Abstract

In this paper we study the statistical geometry of ensembles of poly (L-alanine) conformations computed by several different distance geometry algorithms. Since basic theory only permits us to predict the statistical properties of such ensembles a priori when the distance constraints have a very simple form, the only constraints used for these calculations are those necessary to obtain reasonable bond lengths and angles, together with a lack of short- and long-range atomic overlaps. The geometric properties studied include the squared end-to-end distance and radius of gyration of the computed conformations, in addition to the usual rms coordinate and phi/psi angle deviations among these conformations. The distance geometry algorithms evaluated include several variations of the well-known embed algorithm, together with optimizations of the torsion angles using the ellipsoid and variable target function algorithms. The conclusions may be summarized as follows: First, the distribution with which the trial distances are chosen in most implementations of the embed algorithm is not appropriate when no long-range upper bounds on the distances are present, because it leads to unjustifiably expanded conformations. Second, chosing the trial distances independently of one another leads to a lack of variation in the degree of expansion, which in turn produces a relatively low rms square coordinate difference among the members of the ensemble. Third, when short-range steric constraints are present, torsion angle optimizations that start from conformations obtained by choosing their phi/psi angles randomly with a uniform distribution between -180 degrees and +180 degrees do not converge to conformations whose angles are uniformly distributed over the sterically allowed regions of the phi/psi plane. Finally, in an appendix we show how the sampling obtained with the embed algorithm can be substantially improved upon by the proper application of existing methodology.

MeSH Terms
Algorithms Peptides Protein Conformation
Chemicals
Peptides
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Havel T F
Division of Biophysics, University of Michigan, Ann Arbor 48109.
Article Info
Journal
Biopolymers
Abbr.
Biopolymers
ISSN
0006-3525
Published
1990-00-00
Pages
1565-85
Language
English
Region
United States
NLM ID
0372525
Subset
IM
Grants
NIGMS NIH HHS · GM-37708 · United States
NIGMS NIH HHS · R01 GM-38221 · United States
Analysis Services
Analysis Services

Contact

No. 2 Wenbo Road, Zhangqiu District, Jinan, Shandong

Qilu Normal University · Genelibs Bioinformatics Lab

750 Shunhua Rd, Jinan

2F, Bldg F, University Science Park

Tel: 0531-88819269

WeChat Official Account

Follow our WeChat subscription account for real-time updates and the latest in medical and biological research.


Business Email

E-mail: [email protected]