Real-time NMR investigations of triple-helix folding and collagen folding diseases.
Folding of the collagen triple helix provides an opportunity to look at multichain molecular assembly. This triple helix also offers unique advantages for the study of folding because the process is very slow compared to globular proteins, and the kinetics of folding can be obtained in real time by NMR. Studies on triple-helical peptides illustrate the ability to observe kinetic folding intermediates directly and the ability to propose detailed mechanisms of folding through the use of real-time NMR methods. Defective collagen folding has been implicated in various connective tissue diseases and the capacity of NMR to look at the folding of specific sites provides a tool for obtaining information about altered folding mechanisms. Comparison of folding in peptides that model normal and diseased collagens could shed light on the molecular perturbation and the etiology of disease.
Baum
J
J
Department of Chemistry, Rutgers University, Piscataway, New Jersey 08855-0939, USA. baum@rutchem.rutgers.edu
Brodsky
B
B
D000595:Amino Acid Sequence; D003094:Collagen / Q000737:chemistry / Q000378:metabolism*; D003095:Collagen Diseases / Q000378:metabolism*; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry; D017510:Protein Folding
D010455:Peptides; D003094:Collagen