Titre :
  • Ser and Thr residues modulate the conformation of pro-kinked transmembrane alpha-helices.
Auteur : Deupi, Xavier ; Olivella, Mireia ; Govaerts, Cédric ; Ballesteros, Juan Antonio ; Campillo, Mercedes ; Pardo, Leonardo
Informations sur la publication : Biophysical journal, 86, 1 Pt 1, (page 105-115)
Statut de publication : Publié, 2004-01
Sujet CREF : Sciences bio-médicales et agricoles
Biochimie
Biologie
Biologie cellulaire
Biologie moléculaire
Biophysique
Sciences biomédicales
Sciences de la matière vivante
Mots-clés MeSH : Amino Acid Sequence
Binding Sites
Computer Simulation
Membrane Proteins -- chemistry
Models, Molecular
Molecular Sequence Data
Proline -- chemistry
Protein Binding
Protein Conformation
Protein Structure, Secondary
Receptors, G-Protein-Coupled -- chemistry
Sequence Analysis, Protein -- methods
Sequence Homology, Amino Acid
Serine -- chemistry
Structure-Activity Relationship
Threonine -- chemistry
Note : Comparative Study
Evaluation Studies
Journal Article
Research Support, Non-U.S. Gov't
Validation Studies
SCOPUS: ar.j
Langue :
  • Anglais
Identificateurs : urn:issn:0006-3495 
info:doi/10.1016/S0006-3495(04)74088-6
info:pii/S0006-3495(04)74088-6
info:pmid/14695254
info:pmcid/PMC1303774