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
It is currently believed that the atlas of existing protein structures is faithfully represented in ...
A novel approach, validated by an analysis of barnase and chymotrypsin inhibitor, is introduced to e...
Simple models with a single bead representation (Cα models) have been successful in providing a qual...
A conceptual framework for understanding the protein folding problem has remained elusive in spi...
A framework is presented for understanding the common character of proteins. Proteins are linear cha...
A framework is presented for understanding the common character of proteins. Proteins are linear cha...
We present a model, based on symmetry and geometry, for proteins. Using elementary ideas from mathem...
The native state structures of globular proteins are stable and well packed indicating that self-int...
Recent studies suggest that protein folding should be revisited as the emergent property of a comple...
The size and origin of the protein fold universe is of fundamental and practical importance. Analyzi...
Proteins have a wide array of essential functions: from serving as enzymatic catalysts to protecting...
We present a simple physical model that demonstrates that the native-state folds of proteins can eme...
A novel approach, validated by an analysis of barnase and chymotrypsin inhibitor, is introduced ...
The intricate three-dimensional geometries of protein tertiary structures underlie protein function ...
Under physiological conditions, a protein undergoes a spontaneous disorder reversible arrow order tr...
It is currently believed that the atlas of existing protein structures is faithfully represented in ...
A novel approach, validated by an analysis of barnase and chymotrypsin inhibitor, is introduced to e...
Simple models with a single bead representation (Cα models) have been successful in providing a qual...
A conceptual framework for understanding the protein folding problem has remained elusive in spi...
A framework is presented for understanding the common character of proteins. Proteins are linear cha...
A framework is presented for understanding the common character of proteins. Proteins are linear cha...
We present a model, based on symmetry and geometry, for proteins. Using elementary ideas from mathem...
The native state structures of globular proteins are stable and well packed indicating that self-int...
Recent studies suggest that protein folding should be revisited as the emergent property of a comple...
The size and origin of the protein fold universe is of fundamental and practical importance. Analyzi...
Proteins have a wide array of essential functions: from serving as enzymatic catalysts to protecting...
We present a simple physical model that demonstrates that the native-state folds of proteins can eme...
A novel approach, validated by an analysis of barnase and chymotrypsin inhibitor, is introduced ...
The intricate three-dimensional geometries of protein tertiary structures underlie protein function ...
Under physiological conditions, a protein undergoes a spontaneous disorder reversible arrow order tr...
It is currently believed that the atlas of existing protein structures is faithfully represented in ...
A novel approach, validated by an analysis of barnase and chymotrypsin inhibitor, is introduced to e...
Simple models with a single bead representation (Cα models) have been successful in providing a qual...