Linked Life Data

12781664

Source:http://linkedlifedata.com/resource/pubmed/id/12781664

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2003-6-3
pubmed:abstractText
Atomic force microscopy (AFM) was used to measure the forces stabilizing human aquaporin-1 (hAQP1), a tetrameric transmembrane protein that forms highly specific water channels. To this end, the AFM tip was attached to the C-terminus of hAQP1 and secondary structure elements were extracted from the membrane while the single-molecule force-extension curve was being recorded. Force peaks, reflecting the unfolding of secondary structure elements, could be interpreted in depth using the atomic model of hAQP1. Different classes of force-extension curves indicated the existence of alternative unfolding pathways for individual proteins. In addition, transmembrane helices at the periphery of the hAQP1 tetramer exhibited smaller extraction forces than helices at the interface between hAQP1 monomers. These results represent the first direct assessment of intermolecular forces defining the oligomeric state of a membrane protein.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
1047-8477
pubmed:author
pubmed:issnType
Print
pubmed:volume
142
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
369-78
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2003
pubmed:articleTitle
Determining molecular forces that stabilize human aquaporin-1.
pubmed:affiliation
Max Planck Institute of Molecular Cell Biology and Genetics, Pfotenhauerstrasse 108, 01307 Dresden, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't