Linked Life Data

20932028

Source:http://linkedlifedata.com/resource/pubmed/id/20932028

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
43
pubmed:dateCreated
2010-10-28
pubmed:abstractText
We present a robust solid-state NMR approach for the accurate determination of molecular interfaces in insoluble and noncrystalline protein-protein complexes. The method relies on the measurement of intermolecular (13)C-(13)C distances in mixtures of [1-(13)C]glucose- and [2-(13)C]glucose-labeled proteins. We have applied this method to Parkinson's disease-associated ?-synuclein fibrils and found that they are stacked in a parallel in-register arrangement. Additionally, intermolecular distance restraints for the structure determination of the fibrils at atomic resolution were measured.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
1520-5126
pubmed:author
pubmed:issnType
Electronic
pubmed:day
3
pubmed:volume
132
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
15164-6
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Supramolecular interactions probed by 13C-13C solid-state NMR spectroscopy.
pubmed:affiliation
Department of NMR-Based Structural Biology, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Go?ttingen, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't