title: Sequence dependent conformational variations of collagen triple-helical structure.
abstract: The 2 A crystal structure reported here of the collagen-like model peptide, T3-785, provides the first visualization of how the sequence of collagen defines distinctive local conformational variations in triple-helical structure.
authors.affiliation: Department of Chemistry, Rutgers University, Piscataway, New Jersey 08854-8087, USA.
authors.forename: R Z
authors.initials: RZ
authors.lastname: Kramer
authors.forename: J
authors.initials: J
authors.lastname: Bella
authors.forename: P
authors.initials: P
authors.lastname: Mayville
authors.forename: B
authors.initials: B
authors.lastname: Brodsky
authors.forename: H M
authors.initials: HM
authors.lastname: Berman
mesh_terms: D000595:Amino Acid Sequence; D003094:Collagen / Q000737:chemistry* / Q000378:metabolism; D003460:Crystallization; D018360:Crystallography, X-Ray; D006801:Humans; D006860:Hydrogen Bonding; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry* / Q000378:metabolism; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D016415:Sequence Alignment; D014867:Water / Q000737:chemistry / Q000378:metabolism
chemical_list: D010446:Peptide Fragments; C119065:T3-785 peptide; D014867:Water; D003094:Collagen