Protein folding and unfolding at atomic resolution.
Experiment and simulation are now conspiring to give atomic-level descriptions of protein folding relevant to folding, misfolding, trafficking, and degradation in the cell. We are on the threshold of predicting those protein folding events using simulation that has been carefully benchmarked by experiment.
Fersht
Alan R
AR
Department of Chemistry, MRC Centre for Protein Engineering, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, United Kingdom. arf25@cam.ac.uk
Daggett
Valerie
V
D001426:Bacterial Proteins; D018398:Homeodomain Proteins / Q000737:chemistry; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D010455:Peptides / Q000737:chemistry; D010940:Plant Proteins; D011489:Protein Denaturation; D017510:Protein Folding; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry / Q000378:metabolism*; D012260:Ribonucleases / Q000737:chemistry; D014157:Transcription Factors
D001426:Bacterial Proteins; D018398:Homeodomain Proteins; D010455:Peptides; D010940:Plant Proteins; D011506:Proteins; D014157:Transcription Factors; C093336:chymotrypsin inhibitor 2; C106185:engrailed homeobox proteins; D012260:Ribonucleases; C019760:Bacillus amyloliquefaciens ribonuclease