2005 Emil Thomas Kaiser Award.
Collagen is the most abundant protein in animals. The conformational stability of the collagen triple helix is enhanced by the hydroxyl group of its prevalent (2S,4R)-4-hydroxyproline residues. For 25 years, the prevailing paradigm had been that this enhanced stability is due to hydrogen bonds mediated by bridging water molecules. We tested this hypothesis with synthetic collagen triple helices containing 4-fluoroproline residues. The results have unveiled a wealth of stereoelectronic effects that contribute markedly to the stability of collagen, as well as other proteins. This new understanding is leading to synthetic collagens for a variety of applications in biotechnology and biomedicine.
Raines
Ronald T
RT
Department of Biochemistry, University of Wisconsin-Madison, Madison, Wisconsin 53706-1544, USA. raines@biochem.wisc.edu
D001363:Awards and Prizes; D055598:Chemical Phenomena; D002621:Chemistry; D002942:Circular Dichroism; D003094:Collagen / Q000737:chemistry*; D018360:Crystallography, X-Ray; D018716:Molecular Mimicry; D015394:Molecular Structure; D019906:Nuclear Magnetic Resonance, Biomolecular; D011506:Proteins; D012958:Societies, Scientific; D013329:Structure-Activity Relationship; D014481:United States
D011506:Proteins; D003094:Collagen