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Reading the three‐dimensional structure of lattice model‐designed proteins from their amino acid sequence
Author(s) -
Broglia R.A.,
Tiana G.
Publication year - 2001
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.1158
Subject(s) - amino acid , sequence (biology) , protein folding , lattice (music) , folding (dsp implementation) , peptide sequence , chemistry , lattice protein , physics , protein structure , crystallography , chemical physics , biochemistry , engineering , acoustics , electrical engineering , gene
While all the information required for the folding of a protein is contained in its amino acid sequence, one has not yet learned how to extract this information to predict the detailed, biological active, three‐dimensional structure of a protein whose sequence is known. Using insight obtained from lattice model simulations of the folding of small proteins (fewer than 100 residues), in particular of the fact that this phenomenon is essentially controlled by conserved contacts (Mirny et al., Proc Natl Acad Sci USA 1995;92:1282) among (few) strongly interacting (“hot”) amino acids (Tiana et al., J Chem Phys 1998;108:757–761), which also stabilize local elementary structures formed early in the folding process and leading to the (postcritical) folding core when they assemble together (Broglia et al., Proc Natl Acad Sci USA 1998;95:12930, Broglia & Tiana, J Chem Phys 2001;114:7267), we have worked out a successful strategy for reading the three‐dimensional structure of lattice model‐designed proteins from the knowledge of only their amino acid sequence and of the contact energies among the amino acids. Proteins 2001;45:421–427. © 2001 Wiley‐Liss, Inc.