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Determination of Protein-ligand Interactions Using Differential Scanning Fluorimetry

Determination of Protein-ligand Interactions Using Differential Scanning Fluorimetry

Published on: September 13, 2014

Predicting melting temperature directly from protein sequences.

Tienhsiung Ku¹, Peiyu Lu, Chenhsiung Chan

¹Department of Anesthesiology, Changhua Christian Hospital, Changhua, Taiwan.

Computational Biology and Chemistry

|November 10, 2009

Summary

This summary is machine-generated.

Scientists developed a new method to predict protein melting temperature (Tm) directly from amino acid sequences. This Tm Index tool successfully distinguishes between heat-loving hyperthermophiles and moderate-temperature mesophiles based on their protein sequences.

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A Protocol for Computer-Based Protein Structure and Function Prediction

A Protocol for Computer-Based Protein Structure and Function Prediction

Published on: November 3, 2011

Area of Science:

Proteomics
Bioinformatics
Microbiology

Background:

Proteins in microorganisms are composed of the same 20 amino acids.
Protein thermal tolerance is determined by its amino acid sequence.

Purpose of the Study:

To introduce a rapid method for predicting protein melting temperature (Tm) from amino acid sequences.
To analyze microbial genomes to differentiate between hyperthermophilic and mesophilic organisms.

Main Methods:

Development and application of the Tm Index program for direct Tm prediction from protein sequences.
Analysis of 75 complete microbial genomes using the Tm Index.

Main Results:

The Tm Index successfully differentiated hyperthermophilic from mesophilic microorganisms on a genomic scale.
Results support the hypothesis that hyperthermophiles express more high-Tm proteins than mesophiles.

Conclusions:

The Tm Index provides a valuable tool for predicting protein thermal stability.
This method can aid in modifying existing proteins or designing novel proteins with desired melting temperatures.