rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
1
|
pubmed:dateCreated |
1997-6-24
|
pubmed:abstractText |
How close an approach is necessary for two interactive protein molecules to recognize each other before association? How strong a force field is exerted between two proteins at the recognition distance? How extensive are the association interfaces? How strong a force is necessary to pull the associated proteins apart? By means of atomic force microscopy at a truly single molecule level, these fundamental and intriguing questions were answered with the muscle proteins actin and myosin.
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
May
|
pubmed:issn |
0006-291X
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
8
|
pubmed:volume |
234
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
178-82
|
pubmed:dateRevised |
2008-11-21
|
pubmed:meshHeading |
pubmed-meshheading:9168985-Actins,
pubmed-meshheading:9168985-Animals,
pubmed-meshheading:9168985-Avidin,
pubmed-meshheading:9168985-Biotin,
pubmed-meshheading:9168985-Cadaverine,
pubmed-meshheading:9168985-Chemistry, Physical,
pubmed-meshheading:9168985-Microscopy, Atomic Force,
pubmed-meshheading:9168985-Muscle, Skeletal,
pubmed-meshheading:9168985-Myosin Subfragments,
pubmed-meshheading:9168985-Physicochemical Phenomena,
pubmed-meshheading:9168985-Protein Binding,
pubmed-meshheading:9168985-Rabbits,
pubmed-meshheading:9168985-Transglutaminases
|
pubmed:year |
1997
|
pubmed:articleTitle |
Scanning force microscopy of the interaction events between a single molecule of heavy meromyosin and actin.
|
pubmed:affiliation |
Department of Physics, Faculty of Science, Kanazawa University Kakuma-machi, Japan.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|