NMR and x-ray studies of collagen model peptides.
The main structural component in collagen is the triple helix which is generally composed of the amino acid sequence repeat (X-Y-Gly)n with proline and hydroxyproline often present at positions X and Y. Non-globular, fibrillar proteins like most collagens are difficult to work with from a structural perspective. An alternative approach to collagen structural elucidation is to study considerably shorter fragments of the triple helix. To date, various triple helical model peptides such as (Pro-Pro-Gly)n and (Pro-Hyp-Gly)n have been investigated by various physical and spectroscopic techniques. The advent of easy solid phase peptide synthetic methodology and the development of multi-dimensional heteronuclear and high field NMR technologies have promoted significant advances in the structure elucidation of a number of triple helix peptides. Here, the main focus is to review and to address the current state of knowledge in the field of NMR and x-ray analysis of triple helical model peptides.
Mayo
K H
KH
Department of Biochemistry, University of Minnesota, Minneapolis, 55455, USA.
D000595:Amino Acid Sequence; D003094:Collagen / Q000737:chemistry*; D018360:Crystallography, X-Ray; D009682:Magnetic Resonance Spectroscopy; D008956:Models, Chemical; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry*
D010455:Peptides; D003094:Collagen