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Sequence‐based study of two related proteins with different folding behaviors
Author(s) -
Favrin Giorgio,
Irbäck Anders,
Wallin Stefan
Publication year - 2003
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.10575
Subject(s) - folding (dsp implementation) , sequence (biology) , computational biology , computer science , protein folding , biology , biochemistry , engineering , electrical engineering
Z SPA–1 is an engineered protein that binds to its parent, the three‐helix‐bundle Z domain of staphylococcal protein A. Uncomplexed Z SPA–1 shows a reduced helix content and a melting behavior that is less cooperative, compared with the wild‐type Z domain. Here we show that the difference in folding behavior between these two sequences can be partly understood in terms of an off‐lattice model with 5–6 atoms per amino acid and a minimalistic potential, in which folding is driven by backbone hydrogen bonding and effective hydrophobic attraction. Proteins 2004;54:000–000. © 2003 Wiley‐Liss, Inc.