Measuring the stability of partly folded proteins using TMAO
نویسندگان
چکیده
منابع مشابه
Thermodynamic stability of folded proteins against mutations
By balancing the average energy gap with its typical change due to mutations for protein-like heteropolymers with M residues, we show that native states are unstable to mutations on a scale M ∼ (λ/σμ) 1/ζs , where λ is the dispersion in the interaction free energies and σμ their typical change. Theoretical bounds and numerical estimates (based on complete enumeration on four lattices) of the in...
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The osmolyte trimethylamine N-oxide (TMAO) accumulates in the cell in response to osmotic stress and increases the thermodynamic stability of folded proteins. To understand the mechanism of TMAO induced stabilization of folded protein states, we systematically investigated the action of TMAO on several model dipeptides (leucine, L(2), serine, S(2), glutamine, Q(2), lysine, K(2), and glycine, G(...
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ژورنال
عنوان ژورنال: Protein Science
سال: 2003
ISSN: 0961-8368,1469-896X
DOI: 10.1110/ps.0372903