Related Experiment Video
Updated: May 17, 2025

A New Screening Method for the Directed Evolution of Thermostable Bacteriolytic Enzymes
Published on: November 7, 2012
Prediction and design of thermostable proteins with a desired melting temperature
Purva Tijare1, Nishant Kumar1, Gajendra P S Raghava2
1Department of Computational Biology, Indraprastha Institute of Information Technology, Okhla Industrial Estate, Phase III (Near Govind Puri Metro Station), Office: A-302 (R&D Block), New Delhi, 110020, India.
Abstract:
The stability of proteins at higher temperatures is crucial for their functionality, which is measured by their melting temperature (Tm). The Tm is the temperature at which 50% of the protein loses its native structure and activity. Existing methods for predicting Tm have two major limitations: first, they are often trained on redundant proteins, and second, they do not allow users to design proteins with the desired Tm. To address these limitations, we developed a regression method for predicting the Tm value of proteins using 17,312 non-redundant proteins, where no two proteins are more than 40% similar. We used 80% of the data for training and testing and the remaining 20% for validation. Initially, we developed a machine learning model using standard features from protein sequences. Our best model, developed using Shannon entropy for all residues, achieved the highest Pearson correlation of 0.80 with an R2 of 0.63 between the predicted and actual Tm of proteins on the validation dataset. Next, we fine-tuned large language models (e.g., ProtBert, ProtGPT2, ProtT5) on our training dataset and generated embeddings. These embeddings have been used to develop machine learning models. Our best model, developed using ProtBert embeddings, achieved a maximum correlation of 0.89 with an R2 of 0.80 on the validation dataset. Finally, we developed an ensemble method that combines standard protein features and embeddings. One of the aims of the study is to assist the scientific community in the design of targeted melting temperatures. Our standalone software can be used to screen thermostable proteins at the genome level. We demonstrated the application of PPTstab in identifying thermostable proteins in different organisms. We created a user-friendly web server, and a Python package for predicting and designing thermostable proteins is available at https://webs.iiitd.edu.in/raghava/pptstab , https://github.com/raghavagps/pptstab .
More Related Videos
13:26Determination of Protein-ligand Interactions Using Differential Scanning Fluorimetry
Published on: September 13, 2014
07:22How to Stabilize Protein: Stability Screens for Thermal Shift Assays and Nano Differential Scanning Fluorimetry in the Virus-X Project
Published on: February 11, 2019
Related Concept Videos
Molecular Chaperones and Protein Folding
The...
Protein Folding
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...