Publication Date:
1996-08-02
Description:
Protein structures in nature often exhibit a high degree of regularity (for example, secondary structure and tertiary symmetries) that is absent from random compact conformations. With the use of a simple lattice model of protein folding, it was demonstrated that structural regularities are related to high "designability" and evolutionary stability. The designability of each compact structure is measured by the number of sequences that can design the structure-that is, sequences that possess the structure as their nondegenerate ground state. Compact structures differ markedly in terms of their designability; highly designable structures emerge with a number of associated sequences much larger than the average. These highly designable structures possess "proteinlike" secondary structure and even tertiary symmetries. In addition, they are thermodynamically more stable than other structures. These results suggest that protein structures are selected in nature because they are readily designed and stable against mutations, and that such a selection simultaneously leads to thermodynamic stability.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Li, H -- Helling, R -- Tang, C -- Wingreen, N -- New York, N.Y. -- Science. 1996 Aug 2;273(5275):666-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉NEC Research Institute, 4 Independence Way, Princeton, NJ 08540, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8662562" target="_blank"〉PubMed〈/a〉
Keywords:
*Amino Acid Sequence
;
Evolution, Molecular
;
*Models, Molecular
;
Mutation
;
*Protein Conformation
;
*Protein Folding
;
Protein Structure, Secondary
;
Protein Structure, Tertiary
;
Proteins/*chemistry/genetics
;
Thermodynamics
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
