Sequence‐based study of two related proteins with different folding behaviors | Zendy

Favrin Giorgio | Zendy; Irbäck Anders | Zendy; Wallin Stefan | Zendy

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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.

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