Efficient expansion, folding, and unfolding of proteins.
We consider a nonstatistical, computationally fast experiment to identify important topological constraints in folding small globular proteins of about 100-200 amino acids. In this experiment, proteins are expanded mechanically along a path of steepest increase in the free space around residues. The pathways are often consistent with folding scenarios reported in kinetics experiments and most accurately describe obligatory or mechanic folding proteins. The results suggest that certain topological "defects" in proteins lead to preferred, entropically favorable channels down their free energy landscapes.
Nelson
Erik D
ED
Howard Hughes Medical Institute, University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX 75235-9050, USA. enelson@spirit.sdsc.edu
Grishin
Nick V
NV
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000737:chemistry*; D003198:Computer Simulation; D004548:Elasticity; D008956:Models, Chemical; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011489:Protein Denaturation; D017510:Protein Folding; D011506:Proteins / Q000032:analysis / Q000737:chemistry*; D013329:Structure-Activity Relationship
D000596:Amino Acids; D011506:Proteins