Geometry and physics of proteins.
A conceptual framework for understanding the protein folding problem has remained elusive in spite of many significant advances. We show that geometrical constraints imposed by chain connectivity, compactness, and the avoidance of steric clashes can be encompassed in a natural way using a three-body potential and lead to a selection in structure space, independent of chemical details. Strikingly, secondary motifs such as hairpins, sheets, and helices, which are the building blocks of protein folds, emerge as the chosen structures for segments of the protein backbone based just on elementary geometrical considerations.
Banavar
Jayanth R
JR
Department of Physics, 104 Davey Laboratory, The Pennsylvania State University, University Park, Pennsylvania 16802, USA. banavar@psu.edu
Maritan
Amos
A
Micheletti
Cristian
C
Trovato
Antonio
A
D055592:Biophysical Phenomena; D001703:Biophysics; D008962:Models, Theoretical; D011487:Protein Conformation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry*
D011506:Proteins