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.
|Titolo:||Geometry and physics of proteins|
|Autori:||J.R. BANAVAR; A. MARITAN; MICHELETTI C; A. TROVATO|
|Data di pubblicazione:||2002|
|Digital Object Identifier (DOI):||10.1002/prot.10091|
|Appare nelle tipologie:||1.1 Journal article|