Autor: |
Kulshreshtha S; Amity Institute of Biotechnology, Amity University Rajasthan, 14-Gopal Bari, Ajmer Road, Jaipur, 302006, India. shweta_kulshreshtha@rediffmail.com.; A-200 Vaishali Nagar, Jaipur, 302021, India. shweta_kulshreshtha@rediffmail.com., Chaudhary V; Amity Institute of Biotechnology, Amity University Rajasthan, 14-Gopal Bari, Ajmer Road, Jaipur, 302006, India., Goswami GK; C U Shah Institute of Life Sciences, C U Shah University, Wadhwan City, Surendranagar, Gujarat, 363030, India., Mathur N; Amity Institute of Biotechnology, Amity University Rajasthan, 14-Gopal Bari, Ajmer Road, Jaipur, 302006, India. |
Abstrakt: |
Mutations in the protein affect not only the structure of protein, but also its function and stability. Prediction of mutant protein stability with accuracy is desired for uncovering the molecular aspects of diseases and design of novel proteins. Many advanced computational approaches have been developed over the years, to predict the stability and function of a mutated protein. These approaches based on structure, sequence features and combined features (both structure and sequence features) provide reasonably accurate estimation of the impact of amino acid substitution on stability and function of protein. Recently, consensus tools have been developed by incorporating many tools together, which provide single window results for comparison purpose. In this review, a useful guide for the selection of tools that can be employed in predicting mutated proteins' stability and disease causing capability is provided. |