Document Detail


Developments in low-temperature biochemistry and biology.
MedLine Citation:
PMID:  6131419     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Though under most circumstances harmful changes are induced in cellular structures by subzero temperatures, conditions can be found under which such damage is avoided. Thus, in solution, biochemical reactions can be slowed and more easily analysed and many enzyme-substrate complexes can be stabilized and structurally analysed; in crystals, 'stop-action' pictures unveil the stereochemical changes along reaction pathways. The progressive 'solidification' of non-covalent bonds involved in protein structures should permit investigation of their dynamics. Studies at high pressures open the way to new investigations on 'activated' enzyme-substrate complexes and might permit the refinement of current concepts to a considerable degree, as a preliminary but decisive step towards a full description of enzyme mechanisms. The conditions of medium allowing such cryobiochemical studies fail to protect cellular structures against cold. Investigations of plasma membrane behaviour are now under way to determine processes leading to cryosensitivity or cryotolerance of cells.
Authors:
P Douzou
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Review    
Journal Detail:
Title:  Proceedings of the Royal Society of London. Series B, Containing papers of a Biological character. Royal Society (Great Britain)     Volume:  217     ISSN:  0080-4649     ISO Abbreviation:  Proc. R. Soc. Lond., B, Biol. Sci.     Publication Date:  1982 Dec 
Date Detail:
Created Date:  1983-04-15     Completed Date:  1983-04-15     Revised Date:  2008-11-21    
Medline Journal Info:
Nlm Unique ID:  7505889     Medline TA:  Proc R Soc Lond B Biol Sci     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  1-28     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Animals
Biochemistry / trends*
Biology / trends*
Catalysis
Cold Temperature*
Enzymes / physiology
Microscopy, Electron / methods
Protein Conformation
Thermodynamics
Tissue Preservation
Chemical
Reg. No./Substance:
0/Enzymes

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


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