Thermodynamic Stability of Folded Proteins against Mutations
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 stability of model proteins with designed sequences is assessed in terms of the number of sequences (obtained from the designed sequence through mutations), which fold into the “native” conformation. By a complete enumeration of the total number of sequences obtained by introducing up to 4 point mutations and up to 7 composition–conserving mutations (swapping of amino acids) in a 36mers cha...
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Folded protein structures are both stable and dynamic. Historically, our clearest window into these structures came from X-ray crystallography, which generally provided a static image of each protein's singular "folded state", highlighting its stability. Deviations away from that crystallographic structure were difficult to quantify, and as a result, their potential functional consequences were...
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Vibrational dynamics of folded proteins is studied using a Gaussian model in which the protein is viewed as a network, residues representing the junctions, and the connectivity being established by a single parameter harmonic potential. Application to seven proteins showed that the local packing density plays a major role in determining the vibrational spectrum at time scales of picoseconds. At...
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ژورنال
عنوان ژورنال: Physical Review Letters
سال: 1997
ISSN: 0031-9007,1079-7114
DOI: 10.1103/physrevlett.79.3530