Background: Thermophilic proteins sustain themselves and function at higher temperatures. Despite their structural and functional similarities with their mesophilic homologues, they show enhanced stability. Various comparative studies at genomic, protein sequence and structure levels, and experimental works highlight the different factors and dominant interacting forces contributing to this increased stability. Methods: In this comparative structure based study, we have used interaction energies between amino acids, to generate structure networks called as Protein Energy Networks (PENs). These PENs are used to compute network, sub-graph, and node specific parameters. These parameters are then compared between the thermophile-mesophile homol...
The three-dimensional structure of a protein is formed and maintained by the noncovalent interaction...
<p>* The PDB IDs of Thermophilic (TS), Mesophilic (MS) pair, starting from Column 2, belong to famil...
Background: Gram-negative bacteria use periplasmic-binding proteins (bPBP) to transport nutrients th...
Background: Thermophilic proteins sustain themselves and function at higher temperatures. Despite th...
Thermophilic proteins sustain themselves and function at higher temperatures. Despite their structur...
Understanding the molecular basis for the enhanced stability of proteins from thermophiles has been ...
Understanding the molecular basis for the enhanced stability of proteins from thermophiles has been ...
Understanding the molecular basis for the enhanced stability of proteins from thermophiles has been ...
AbstractBackground: Proteins from thermophilic organisms usually show high intrinsic thermal stabili...
Protein thermostability is an important field for its evolutionary perspective of mesophilic versus ...
AbstractThis study views each protein structure as a network of noncovalent connections between amin...
This study views each protein structure as a network of noncovalent connections between amino acid s...
This study views each protein structure as a network of noncovalent connections between amino acid s...
Motivation: Understanding the molecular mechanisms of thermal stability is a challenge in protein bi...
Studies of the structural basis of protein thermostability have produced a confusing picture. Small ...
The three-dimensional structure of a protein is formed and maintained by the noncovalent interaction...
<p>* The PDB IDs of Thermophilic (TS), Mesophilic (MS) pair, starting from Column 2, belong to famil...
Background: Gram-negative bacteria use periplasmic-binding proteins (bPBP) to transport nutrients th...
Background: Thermophilic proteins sustain themselves and function at higher temperatures. Despite th...
Thermophilic proteins sustain themselves and function at higher temperatures. Despite their structur...
Understanding the molecular basis for the enhanced stability of proteins from thermophiles has been ...
Understanding the molecular basis for the enhanced stability of proteins from thermophiles has been ...
Understanding the molecular basis for the enhanced stability of proteins from thermophiles has been ...
AbstractBackground: Proteins from thermophilic organisms usually show high intrinsic thermal stabili...
Protein thermostability is an important field for its evolutionary perspective of mesophilic versus ...
AbstractThis study views each protein structure as a network of noncovalent connections between amin...
This study views each protein structure as a network of noncovalent connections between amino acid s...
This study views each protein structure as a network of noncovalent connections between amino acid s...
Motivation: Understanding the molecular mechanisms of thermal stability is a challenge in protein bi...
Studies of the structural basis of protein thermostability have produced a confusing picture. Small ...
The three-dimensional structure of a protein is formed and maintained by the noncovalent interaction...
<p>* The PDB IDs of Thermophilic (TS), Mesophilic (MS) pair, starting from Column 2, belong to famil...
Background: Gram-negative bacteria use periplasmic-binding proteins (bPBP) to transport nutrients th...