Thermostable proteins have many applications. They have utility in food and
beverages, paper and pulp industries, animal feed production, laundry and detergent,
and molecular biology and diagnostics. Many factors contribute to protein
thermostability. These include covalent and non-covalent interactions, protein folding
and conformation, and other thermodynamic factors. Although the available protein
structures have been increasing over time, the increase in available protein sequences is
overwhelmingly enormous. Also, structure determination can be a challenging job and
many proteins are difficult to crystallize. This has resulted in a sequence-structure gap.
The use of computer-assisted structure prediction has helped in filling this gap. There
are many in silico strategies and methods available to predict and analyze protein
structure and properties. These can be used to determine protein stability and are quite
useful for in silico protein analysis to improve function and thermostability.
Keywords: In silico, Molecular dynamics, Mutagenesis, Protein thermostability,
Rational design.
