Bound water in the collagen-like triple-helical structure.
The ir amide bands of the triple-helical polytripeptides and collagens upon hydration of films are investigated. On the basis of our assignment of the amide I components, the formation of hydrogen bonds between the peptide backbone and structural water is studied. The C1O1--HOH hydrogen bonds are found more ordered than the C3O3--HOH hydrogen bonds. The specific incorporation of water in the triple helix is followed by multistep conformational changes and by increasing of the interpeptide hydrogen-bond strength. The formation of the polypeptide hydrate structure depending on the amino acid composition and the chain length is examined.
Lazarev
Y A
YA
Institute of Cell Biophysics, Academy of Sciences of the USSR, Pushchino, Moscow Region.
Grishkovsky
B A
BA
Khromova
T B
TB
Lazareva
A V
AV
Grechishko
V S
VS
D000595:Amino Acid Sequence; D003094:Collagen / Q000737:chemistry*; D006860:Hydrogen Bonding; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry*; D011487:Protein Conformation; D014867:Water / Q000737:chemistry*
D010455:Peptides; D014867:Water; C070969:benzyloxycarbonyl- (glycyl-prolyl-proline)8- methyl ester; D003094:Collagen