2003/09/19 by Canan Baysal, Ali Rana Atılgan, Baysal, Canan +2
Biochemistry, Genetics and Molecular Biology · Materials Science · Physics and Astronomy · #Biomolecules (q-bio.BM) #Enzyme Structure and Function #FOS: Biological sciences #FOS: Physical sciences #Origins and Evolution of Life #Protein Structure and Dynamics #Soft Condensed Matter (cond-mat.soft) #cond-mat.soft #q-bio.BM
paper · pdf · doi:10.48550/arxiv.cond-mat/0309448
13 pages with 4 figures; submitted to Phys. Rev. Lett
arxiv created 2003/09/19 · openalex publication_date 2003/09/19 · arxiv updated 2009/12/01 · openalex created_date 2025/10/10 · openalex updated_date 2026/07/28
We provide evidence that the energy landscapes of folded proteins do not shift with temperature, but the onset of functional dynamics is associated with its effective sampling. The motion of the backbone is described by three distinct regimes. One is associated with slow time scales of the activity along the envelope of the energy surface defining the folded protein. Another, with fast time scales, is due to activity along the pockets decorating the folded-state envelope. The intermediate regime emerges at temperatures where jumps between the pockets become possible, leading to an active protein.