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Computer simulations of the properties of the α 2 , α 2 C, and α 2 D de novo designed helical proteins
Author(s) -
Sikorski Andrzej,
Kolinski Andrzej,
Skolnick Jeffrey
Publication year - 2000
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/(sici)1097-0134(20000101)38:1<17::aid-prot3>3.0.co;2-v
Subject(s) - protein folding , crossover , crystallography , bundle , helix (gastropod) , helix bundle , folding (dsp implementation) , chemistry , biophysics , protein structure , chemical physics , materials science , biology , biochemistry , computer science , engineering , ecology , artificial intelligence , snail , electrical engineering , composite material
Reduced lattice models of the three de novo designed helical proteins α 2 , α 2 C, and α 2 D were studied. Low temperature stable folds were obtained for all three proteins. In all cases, the lowest energy folds were four‐helix bundles. The folding pathway is qualitatively the same for all proteins studied. The energies of various topologies are similar, especially for the α 2 polypeptide. The simulated crossover from molten globule to native‐like behavior is very similar to that seen in experimental studies. Simulations on a reduced protein model reproduce most of the experimental properties of the α 2 , α 2 C, and α 2 D proteins. Stable four‐helix bundle structures were obtained, with increasing native‐like behavior on‐going from α 2 to α 2 D that mimics experiment. Proteins 2000;38:17–28. ©2000 Wiley‐Liss, Inc.