2003/03/28 by Ned Wingreen, Hao Li, Wingreen, Ned +3
Biochemistry, Genetics and Molecular Biology · Physics and Astronomy · #Biological Physics (physics.bio-ph) #Biomolecules (q-bio.BM) #FOS: Biological sciences #FOS: Physical sciences #Soft Condensed Matter (cond-mat.soft) #Statistical Mechanics (cond-mat.stat-mech) #cond-mat.soft #cond-mat.stat-mech #physics.bio-ph #q-bio.BM
paper · pdf · doi:10.48550/arxiv.cond-mat/0303600
12 pages, 10 figures, a review to be published in Polymer
arxiv created 2003/03/28 · arxiv updated 2009/11/30
Only about 1,000 qualitatively different protein folds are believed to exist in nature. Here, we review theoretical studies which suggest that some folds are intrinsically more designable than others, \it i.e. are lowest energy states of an unusually large number of sequences. The sequences associated with these folds are also found to be unusually thermally stable. The connection between highly designable structures and highly stable sequences is generally known as the "designability principle". The designability principle may help explain the small number of natural folds, and may also guide the design of new folds.