Insights on the conformational stability of collagen.
This review describes work on the conformational stability of the collagen triple helix. In 1994, the structure of collagen was determined at high resolution. Since then, much work has been done on synthetic mimics of collagen that contain host-guest peptides, tethers, peptoid residues, or analogs of the prevalent 4(R)-hydroxy-L-proline residues. This work has revealed much about the chemical basis for collagen stability, and could spawn useful new biomaterials. The literature from 1994 to mid 2001 is reviewed, and 116 references are cited.
Jenkins
Cara L
CL
Department of Chemistry, University of Wisconsin-Madison, 53706, USA.
Raines
Ronald T
RT
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis*; D003094:Collagen / Q000737:chemistry*; D005461:Fluorine / Q000737:chemistry; D006801:Humans; D006909:Hydroxyproline / Q000032:analysis*; D018716:Molecular Mimicry; D015394:Molecular Structure; D019906:Nuclear Magnetic Resonance, Biomolecular; D034444:Peptoids; D011392:Proline / Q000737:chemistry; D011487:Protein Conformation; D014961:X-Ray Diffraction
D000596:Amino Acids; D034444:Peptoids; D005461:Fluorine; D003094:Collagen; D011392:Proline; D006909:Hydroxyproline