Predicting protein stability and solubility changes upon mutations: data perspective
نویسندگان
چکیده
منابع مشابه
CUPSAT: Predicting Protein Stability Upon Point Mutations
CUPSAT is a web tool to analyse and predict protein stability changes upon point mutations (single amino acid mutations) in proteins. These mutations are carried out experimentally using site-directed mutagenesis and similar techniques. Random mutations at a specified position aid in designing thermostable or thermosensitive proteins so that the functionality of a protein can be altered to suit...
متن کاملPredicting protein thermostability changes from sequence upon multiple mutations
MOTIVATION A basic question in protein science is to which extent mutations affect protein thermostability. This knowledge would be particularly relevant for engineering thermostable enzymes. In several experimental approaches, this issue has been serendipitously addressed. It would be therefore convenient providing a computational method that predicts when a given protein mutant is more thermo...
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The accurate prediction of the impact of an amino acid substitution on the thermal stability of a protein is a central issue in protein science, and is of key relevance for the rational optimization of various bioprocesses that use enzymes in unusual conditions. Here we present one of the first computational tools to predict the change in melting temperature ΔTm upon point mutations, given the ...
متن کاملiPTREE-STAB: interpretable decision tree based method for predicting protein stability changes upon mutations
UNLABELLED We have developed a web server, iPTREE-STAB for discriminating the stability of proteins (stabilizing or destabilizing) and predicting their stability changes (delta deltaG) upon single amino acid substitutions from amino acid sequence. The discrimination and prediction are mainly based on decision tree coupled with adaptive boosting algorithm, and classification and regression tree,...
متن کاملA neural-network-based method for predicting protein stability changes upon single point mutations
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...
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ژورنال
عنوان ژورنال: ChemCatChem
سال: 2020
ISSN: 1867-3880,1867-3899
DOI: 10.1002/cctc.202000933