Discrimination of thermophilic and mesophilic proteins

Abstract

Background There is a considerable literature on the source of the thermostability of proteins from thermophilic organisms. Understanding the mechanisms for this thermostability would provide insights into proteins generally and permit the design of synthetic hyperstable biocatalysts.Results We have systematically tested a large number of sequence and structure derived quantities for their ability to discriminate thermostable proteins from their non-thermostable orthologs using sets of mesophile-thermophile ortholog pairs. Most of the quantities tested correspond to properties previously reported to be associated with thermostability. Many of the structure related properties were derived from the Delaunay tessellation of protein structures.Conclusions Carefully selected sequence based indices discriminate better than purely structure based indices. Combined sequence and structure based indices improve performance somewhat further. Based on our analysis, the strongest contributors to thermostability are an increase in ion pairs on the protein surface and a more strongly hydrophobic interior.

Bioprospecting thermostable cellulosomes for efficient biofuel production from lignocellulosic biomass

“…Hydrogen bonding between the chains makes the structure of lignocellulosic biomass very rigid and recalcitrant (Yamada et al 2013). Thermostable cellulases are characterized by hydrophobic protein core and polarity at the surface; compact structure with lesser internal voids; higher content of proline and lesser content of asparagines, glutamine, methionine and cysteine; increased level of H-bonding, isoelectric points and salt bridges (Taylor and Vaisman 2010;Li et al 2011).…”

A Novel Statistical Method for Thermostable Proteins Discrimination

“…We have computed several sequence based numerical indices, based on the quantities that www.ijorcs.org other authors have reported that are associated with thermostability. We tested their ability to successfully discriminate between thermophile/mesophile pairs [2].…”

“…In second mode, dipeptide composition frequencies; in third mode, physical-chemical features of table (2) and in forth mode, all the previous features were used to build feature vector of samples. We applied this division to study the effect of different bunches of features on discrimination power and evaluation measures.…”

“…Initial research conducted in the field of protein thermal stability dates back to three decades ago [2]. The reason is that thermal instability of proteins at high temperature is a barrier against the functional development of proteins.…”

“…There are twenty amino acid types that occur in living things [2,3]. Amino acids are sometimes called residues when covalently bonded together to form a protein molecule.…”