Abstract
AbstractA space‐filling model of collagen has been constructed in accordance with the conformation found for (Gly.Pro.Pro)n. The model shows that leucyl and phenylalanyl residues can be easily accommodated at position X of the collagen tripeptide sequence Gly.X.Y, but are severely constrained by steric hindrance at position Y. Examination of the model has also led to the suggestion that hydrogen bonding of hydroxyproline OH through a water molecule to glycyl CO on the same polypeptide chain might account for the stabilisation of the triple helix conformation by hydroxyproline.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
