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
MeSH keywords: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 générale: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:scp/0347949636
info:pmid/14695254
PMC1303774