Physics of proteins.
Globular proteins are a key component of the network of life. Over many decades much experimental data on proteins have been gathered, yet theoretical progress has been somewhat limited. We show that the results accumulated over the years inexorably lead to a unified framework for understanding proteins. The framework predicts the existence of a fixed menu of folds determined by geometry, clarifies the role of the amino acid sequence in selecting the native-state structure from this menu, and explains the propensity for amyloid formation. The experimental data and the new approach reveal an astonishing simplicity underlying the protein problem.
Banavar
Jayanth R
JR
Department of Physics, The Pennsylvania State University, University Park, Pennsylvania 16802, USA. jayanth@phys.psu.edu
Maritan
Amos
A
D000682:Amyloid / Q000737:chemistry*; D000818:Animals; D001703:Biophysics / Q000379:methods*; D019143:Evolution, Molecular; D006801:Humans; D008962:Models, Theoretical; D036103:Nanotechnology / Q000379:methods; D011487:Protein Conformation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry*; D040901:Proteomics / Q000379:methods; D013816:Thermodynamics
D000682:Amyloid; D011506:Proteins