Linked Life Data

15653834

Source:http://linkedlifedata.com/resource/pubmed/id/15653834

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2005-1-17
pubmed:abstractText
Single-molecule fluorescence methods provide new tools for the study of biological systems. Single-pair fluorescence resonance energy transfer has provided detailed information about dynamics and structure of the Ca2+-signaling protein calmodulin. Single-molecule polarization modulation spectroscopy has probed the mechanism by which calmodulin activates the plasma membrane Ca2+ pump.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
1548-9213
pubmed:author
pubmed:issnType
Print
pubmed:volume
20
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
10-4
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:year
2005
pubmed:articleTitle
Single-molecule fluorescence spectroscopy: new probes of protein function and dynamics.
pubmed:affiliation
Department of Chemistry, University of Kansas, Lawrence, Kansas 66045, USA. ckjohnson@ku.edu
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Review