2003/01/30 by G. Tiana, Guido Tiana, F. Simona +11
Agricultural and Biological Sciences · Biochemistry, Genetics and Molecular Biology · Materials Science · Physics and Astronomy · #Enzyme Structure and Function #FOS: Biological sciences #FOS: Physical sciences #Protein Structure and Dynamics #Proteins in Food Systems #Quantitative Biology (q-bio) #Soft Condensed Matter (cond-mat.soft) #cond-mat.soft #q-bio
paper · pdf · doi:10.48550/arxiv.cond-mat/0301582
arxiv created 2003/01/30 · openalex publication_date 2003/01/30 · arxiv updated 2009/11/30 · openalex created_date 2019/06/27 · openalex updated_date 2026/07/28
The results of minimal model calculations suggest that the stability and the kinetic accessibility of the native state of small globular proteins are controlled by few "hot" sites. By mean of molecular dynamics simulations around the native conformation, which simulate the protein and the surrounding solvent at full--atom level, we generate an energetic map of the equilibrium state of the protein and simplify it with an Eigenvalue decomposition. The components of the Eigenvector associated with the lowest Eigenvalue indicate which are the "hot" sites responsible for the stability and for the fast folding of the protein. Comparison of these predictions with the results of mutatgenesis experiments, performed for five small proteins, provide an excellent agreement.