Linked Life Data

15121092

Source:http://linkedlifedata.com/resource/pubmed/id/15121092

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2004-5-3
pubmed:abstractText
To understand how red blood cell and other proteins carry out their functions, it is necessary not only to have high-resolution crystal structures, but also to have methods that can measure changes in position of parts of the protein on the scale of Angstroms. The method of luminescence resonance energy transfer (LRET) has considerable advantages for this purpose, particularly for proteins, such as the AE1 anion exchange protein in the red cell, that are homodimers. We have applied this method, using a terbium maleimide chelate (TbM) as donor and fluorescein maleimide (FM) as acceptor, to measure the distance between the C201 residues in adjacent dimerized cytoplasmic domains of AE1 (cdAE1). The distance measured by LRET (40.8 A) corresponds closely with that calculated from the crystal structure of the cdAE1, indicating that the method can provide useful information for testing hypotheses concerning motions in this and other blood cell proteins.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1079-9796
pubmed:author
pubmed:issnType
Print
pubmed:volume
32
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
360-5
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:articleTitle
Use of luminescence resonance energy transfer to measure distances in the AE1 anion exchange protein dimer.
pubmed:affiliation
Department of Biochemistry and Biophysics, University of Rochester Medical Center, Medical Center 2-6820, 601 Elmwood Avenue, Rochester, NY 14642, USA. Philip.knauf@urmc.rochester.edu
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.