From protein folding to protein function and biomolecular binding by energy landscape theory.
Protein folding and function are inherently linked sharing a joined funneled energy landscape. In this theoretical framework, the integration of simulations, structural information, and sequence data has led to quantitatively explore, understand, and predict biomolecular binding and recognition, key processes in pharmacology, as a natural extension of the selective self-binding found in protein folding. Computer simulations based on these principles have made valuable contributions to understanding protein and RNA folding, protein-protein interactions, and protein-metabolite/RNA-metabolite interactions.
Department of Chemistry, Umeå University, Umeå, Sweden.
Alexander
A
Schug
José N
JN
Onuchic
D000495:Allosteric Site; D003198:Computer Simulation; D015195:Drug Design; D008958:Models, Molecular; D011485:Protein Binding; D011487:Protein Conformation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry* / Q000235:genetics / Q000502:physiology*; D015398:Signal Transduction; D013696:Temperature; D013816:Thermodynamics
D011506:Proteins