2005/09/16 by Sanghyun Park, Randall J. Radmer, Teri E. Klein +1 · 1 citation
Materials Science · Biochemistry, Genetics and Molecular Biology · Chemistry · #Collagen: Extraction and Characterization #Chemical Synthesis and Analysis #Hydroxyproline #Molecular mechanics #Hydroxylation #Molecular dynamics #Chemistry #Context (archaeology) #Proline #Collagen helix #Monomer #Computational chemistry #Triple helix #Stereochemistry #Amino acid #Biochemistry #Enzyme #Biology #Organic chemistry #Polymer
paper · doi:10.1002/jcc.20301
openalex publication_date 2005/09/16 · openalex created_date 2025/10/10 · openalex updated_date 2026/06/24
Recently, the importance of proline ring pucker conformations in collagen has been suggested in the context of hydroxylation of prolines. The previous molecular mechanics parameters for hydroxyproline, however, do not reproduce the correct pucker preference. We have developed a new set of parameters that reproduces the correct pucker preference. Our molecular dynamics simulations of proline and hydroxyproline monomers as well as collagen-like peptides, using the new parameters, support the theory that the role of hydroxylation in collagen is to stabilize the triple helix by adjusting to the right pucker conformation (and thus the right phi angle) in the Y position.