Document Detail


Macromolecular assemblies: greater than their parts.
MedLine Citation:
PMID:  11179899     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Increasingly powerful methods of analysis have opened up complex macromolecular assemblies to scrutiny at atomic detail. They reveal not only examples of assembly from preformed and prefolded components, but also examples in which the act of assembly drives changes to the components. In the most extreme of these examples, some of the components only achieve a folded state when the complex is formed. Striking results have appeared for systems ranging from the already mature field of virus structure and assembly, where notable progress has been made for rather complex capsids, to descriptions of ribosome structures in atomic detail, where recent results have emerged at breathtaking speed.
Authors:
D H Bamford; R J Gilbert; J M Grimes; D I Stuart
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Publication Detail:
Type:  Journal Article; Review    
Journal Detail:
Title:  Current opinion in structural biology     Volume:  11     ISSN:  0959-440X     ISO Abbreviation:  Curr. Opin. Struct. Biol.     Publication Date:  2001 Feb 
Date Detail:
Created Date:  2001-02-22     Completed Date:  2001-05-10     Revised Date:  2005-11-16    
Medline Journal Info:
Nlm Unique ID:  9107784     Medline TA:  Curr Opin Struct Biol     Country:  England    
Other Details:
Languages:  eng     Pagination:  107-13     Citation Subset:  IM    
Affiliation:
Institute of Biotechnology and Department of Biosciences, Biocentre 2 (room 6002), PO Box 56 (Viikinkaari 5), 00014 University of Helsinki, Helsinki, Finland.
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MeSH Terms
Descriptor/Qualifier:
Crystallography
Macromolecular Substances
Microscopy, Electron
Models, Molecular
Nucleic Acid Conformation
Protein Conformation
Ribosomes / chemistry*,  metabolism
Virus Assembly*
Viruses / chemistry*
Chemical
Reg. No./Substance:
0/Macromolecular Substances

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


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