Bound water in the collagen‐like triple‐helical structure

Abstract 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 C 1 O 1 —HOH hydrogen bonds are found more ordered than the C 3 O 3 —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.