Inter-chain proline:proline contacts contribute to the stability of the triple helical conformation.
The triple helical conformation observed in the collagen group of proteins is related to the presence of large numbers of imino residues and is derived from the stereochemical properties of these residues. The triple helix is stabilized by increasing numbers of these residues. Hydrogen bonds are usually considered to be a major factor in the formation and stability of protein conformation, however, imino residues are not hydrogen bond donors. We have evaluated the role of these residues in stabilizing the triple helix by re-examining two X-ray based structures of the triple helical polypeptide (Pro-Pro-Gly)10 using molecular mechanics calculations. The two minimized structures are comparable in energy and have helical parameters close to the starting values for each starting structure. Our studies suggest that clusters of close van der Waals contacts between proline residues in adjacent chains contribute significantly to the stability of the triple helix. Preliminary NMR studies support this concept. We propose that non-bonded interactions between proline residues may be a significant stabilizing force in the triple helix generated by (Pro-Pro-Gly)10.
Bhatnagar
R S
RS
Laboratory of Connective Tissue Biochemistry, School of Dentistry University of California San Francisco 94143.
Pattabiraman
N
N
Sorensen
K R
KR
Langridge
R
R
MacElroy
R D
RD
Renugopalakrishnan
V
V
D055598:Chemical Phenomena; D002627:Chemistry, Physical; D005998:Glycine; D006860:Hydrogen Bonding; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D010455:Peptides; D011392:Proline; D011487:Protein Conformation
D010455:Peptides; D011392:Proline; D005998:Glycine