STRUM: structure-based prediction of protein stability changes upon single-point mutation
نویسندگان
چکیده
منابع مشابه
STRUM: structure-based prediction of protein stability changes upon single-point mutation
MOTIVATION Mutations in human genome are mainly through single nucleotide polymorphism, some of which can affect stability and function of proteins, causing human diseases. Several methods have been proposed to predict the effect of mutations on protein stability; but most require features from experimental structure. Given the fast progress in protein structure prediction, this work explores t...
متن کاملPrediction of protein stability upon point mutations.
Prediction of protein stability upon amino acid substitution is a challenging problem and it will be helpful for designing stable mutants. We have developed a thermodynamic database for proteins and mutants (ProTherm), which has more than 20000 thermodynamic data along with sequence and structure information, experimental conditions and literature information. It is freely accessible at http://...
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Identifying the contributions to thermodynamic stability of capsids is of fundamental and practical importance. Here we use simulation to assess how mutations affect the stability of lumazine synthase from the hyperthermophile Aquifex aeolicus, a T = 1 icosahedral capsid; in the simulations the icosahedral symmetry of the capsid is preserved by simulating a single pentamer and imposing crystal ...
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MOTIVATION One important requirement for protein design is to be able to predict changes of protein stability upon mutation. Different methods addressing this task have been described and their performance tested considering global linear correlation between predicted and experimental data. Neither is direct statistical evaluation of their prediction performance available, nor is a direct compa...
متن کاملCUPSAT: prediction of protein stability upon point mutations
CUPSAT (Cologne University Protein Stability Analysis Tool) is a web tool to analyse and predict protein stability changes upon point mutations (single amino acid mutations). This program uses structural environment specific atom potentials and torsion angle potentials to predict DeltaDeltaG, the difference in free energy of unfolding between wild-type and mutant proteins. It requires the prote...
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ژورنال
عنوان ژورنال: Bioinformatics
سال: 2016
ISSN: 1367-4803,1460-2059
DOI: 10.1093/bioinformatics/btw361