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PMID: 7663342 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Predicting the helix packing of globular proteins by self-correcting distance geometry.

Protein science : a publication of the Protein Society ·Vol. 4 ·No. 5 ·1995-05-00 ·Pages 863-71

Mumenthaler C, Braun W

Abstract

A new self-correcting distance geometry method for predicting the three-dimensional structure of small globular proteins was assessed with a test set of 8 helical proteins. With the knowledge of the amino acid sequence and the helical segments, our completely automated method calculated the correct backbone topology of six proteins. The accuracy of the predicted structures ranged from 2.3 A to 3.1 A for the helical segments compared to the experimentally determined structures. For two proteins, the predicted constraints were not restrictive enough to yield a conclusive prediction. The method can be applied to all small globular proteins, provided the secondary structure is known from NMR analysis or can be predicted with high reliability.

MeSH Terms
Amino Acid Sequence Calbindins Computer Graphics Crystallography, X-Ray Databases, Factual Hemerythrin/chemistry Magnetic Resonance Spectroscopy Molecular Structure Protein Conformation Protein Structure, Secondary Protein Structure, Tertiary Proteins/chemistry S100 Calcium Binding Protein G/chemistry Software
Chemicals
Calbindins Hemerythrin Proteins S100 Calcium Binding Protein G
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Mumenthaler C
Institut für Molekularbiologie und Biophysik, Eidgenössische Technische Hochschule-Hönggerberg, Zürich, Switzerland.
Braun W
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Article Info
Journal
Protein science : a publication of the Protein Society
Abbr.
Protein Sci
ISSN
0961-8368
DOI
10.1002/pro.5560040506
Published
1995-05-00
Pages
863-71
Language
English
Region
United States
NLM ID
9211750
PMCID
PMC2143125
Subset
IM
External Links
PubMed source DOI: 10.1002/pro.5560040506 PMC Full Text View journal details
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