rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
1
|
pubmed:dateCreated |
1996-6-27
|
pubmed:abstractText |
Many biochemists would regard pressure as a physical parameter mainly of theoretical interest and of rather limited value in experimental biochemistry. The goal of this overview is to show that pressure is a powerful tool for the study of proteins and modulation of enzymatic activity.
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Jan
|
pubmed:issn |
0887-3585
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:volume |
24
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
81-91
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading |
pubmed-meshheading:8628735-Biophysics,
pubmed-meshheading:8628735-DNA,
pubmed-meshheading:8628735-Hydrogen Bonding,
pubmed-meshheading:8628735-Hydrostatic Pressure,
pubmed-meshheading:8628735-Models, Molecular,
pubmed-meshheading:8628735-Molecular Structure,
pubmed-meshheading:8628735-Protein Conformation,
pubmed-meshheading:8628735-Protein Denaturation,
pubmed-meshheading:8628735-Proteins,
pubmed-meshheading:8628735-Structure-Activity Relationship,
pubmed-meshheading:8628735-Temperature
|
pubmed:year |
1996
|
pubmed:articleTitle |
High pressure effects on protein structure and function.
|
pubmed:affiliation |
Institut National de la Santé et de la Recherche Médicale, INSERM U 128, Montpellier, France.
|
pubmed:publicationType |
Journal Article,
Review,
Research Support, Non-U.S. Gov't
|