Sequence dependent conformational variations of collagen triple-helical structure.
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.
Kramer
R Z
RZ
Department of Chemistry, Rutgers University, Piscataway, New Jersey 08854-8087, USA.
Bella
J
J
Mayville
P
P
Brodsky
B
B
Berman
H M
HM
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
D010446:Peptide Fragments; C119065:T3-785 peptide; D014867:Water; D003094:Collagen