Geometry and symmetry presculpt the free-energy landscape of proteins.
We present a simple physical model that demonstrates that the native-state folds of proteins can emerge on the basis of considerations of geometry and symmetry. We show that the inherent anisotropy of a chain molecule, the geometrical and energetic constraints placed by the hydrogen bonds and sterics, and hydrophobicity are sufficient to yield a free-energy landscape with broad minima even for a homopolymer. These minima correspond to marginally compact structures comprising the menu of folds that proteins choose from to house their native states in. Our results provide a general framework for understanding the common characteristics of globular proteins.
Hoang
Trinh Xuan
TX
Institute of Physics, National Centre for Natural Science and Technology, 46 Nguyen Van Ngoc, Hanoi, Vietnam.
Trovato
Antonio
A
Seno
Flavio
F
Banavar
Jayanth R
JR
Maritan
Amos
A
D016880:Anisotropy; D006860:Hydrogen Bonding; D057927:Hydrophobic and Hydrophilic Interactions; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism*; D013696:Temperature; D013816:Thermodynamics
D011506:Proteins