title: Geometry and symmetry presculpt the free-energy landscape of proteins.
abstract: 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.
authors.affiliation: Institute of Physics, National Centre for Natural Science and Technology, 46 Nguyen Van Ngoc, Hanoi, Vietnam.
authors.forename: Trinh Xuan
authors.initials: TX
authors.lastname: Hoang
authors.forename: Antonio
authors.initials: A
authors.lastname: Trovato
authors.forename: Flavio
authors.initials: F
authors.lastname: Seno
authors.forename: Jayanth R
authors.initials: JR
authors.lastname: Banavar
authors.forename: Amos
authors.initials: A
authors.lastname: Maritan
mesh_terms: D016880:Anisotropy; D006860:Hydrogen Bonding; D057927:Hydrophobic and Hydrophilic Interactions; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism*; D013696:Temperature; D013816:Thermodynamics
chemical_list: D011506:Proteins