Protein Thermostability Is Owing to Their Preferences to Non-Polar Smaller Volume Amino Acids, Variations in Residual Physico-Chemical Properties and More Salt-Bridges
Inferred edges come from two machine sources: sweeps of open repository
metadata (mostly SSRN and Zenodo), and a bulk OpenAlex citation snapshot. Every row below is
labelled with the one it came from. Neither is a complete citation index — absence here is not
evidence of absence.
Is this your work? Sign in with ORCID and put your name on the
claims that are yours.
Reference health. See whether every reference in this work resolves to a
known work and none has been retracted — and get a dated CiteStamped
badge you can embed.
Protein Thermostabilizing Factors: High Relative Occurrence of Amino Acids, Residual Properties, and Secondary Structure Type in Different Residual State
Comparative analysis of protein thermostability: Differences in amino acid content and substitution at the surfaces and in the core regions of thermophilic and mesophilic proteins
Determinants of Enzyme Thermostability Observed in the Molecular Structure ofThermusaquaticus d -Glyceraldehyde-3-phosphate Dehydrogenase at 2.5 Å Resolution,
Contribution of a Salt Bridge to the Thermostability of DNA Binding Protein HU from Bacillus stearothermophilus Determined by Site-Directed Mutagenesis
A generalized machine‐learning aided method for targeted identification of industrial enzymes from metagenome: A xylanase temperature dependence case study
Converting the genomic knowledge base to build protein specific machine learning prediction models; a classification study on thermophilic serine protease
Adaptations, diversity, and biotechnological potential of thermophilic microorganisms: exploring culture-dependent and culture-independent approaches in extreme environments
Strategies for enhanced acetone-butanol-ethanol production by Clostridium beijerinckii Y10 from glucose and xylose and exploration of its physiological mechanisms
Higher peptide nonplanarity (ω) close to protein carboxy-terminal and its positive correlation with ψ dihedral-angle is evolved conferring protein thermostability
Meltome Atlas of Arabidopsis thaliana proteome: a melting temperature-based identification of heat and cold resistant proteins using in-silico approach
A scalable overexpression of a thermostable recombinant poly-histidine tag carboxyl esterase under lambda promoter: purification, characterization, and protein modelling
Comprehensive mutagenesis to identify amino acid residues contributing to the difference in thermostability between two originally thermostable ancestral proteins
In vitro and in silico analyses of amino acid substitution effects at the conserved N-linked glycosylation site in hepatitis B virus surface protein on antigenicity, immunogenicity, HBV replication and secretion
Purification and Characterization of Natural Solid-Substrate Degrading and Alcohol Producing Hyperthermostable Alkaline Amylase from Bacillus cereus (sm-sr14)
A Single Point Mutation Controls the Rate of Interconversion Between the g+ and g− Rotamers of the Histidine 189 χ2 Angle That Activates Bacterial Enzyme I for Catalysis
Purification and Structural Characterization of the Auxiliary Activity 9 Native Lytic Polysaccharide Monooxygenase from Thermoascus aurantiacus and Identification of Its C1- and C4-Oxidized Reaction Products
Peptides on a rescue mission against the hazardous cidal chemicals used in Eastern Indian Agriculture: An in-silico approach based on field survey in 2020
Amino acid frequency and domain features serve well for random forest based classification of thermophilic and mesophilic protein; a case study on serine proteases
Dynamique spatiale et temporelle des communautés mircrobiennes dans les édifices hydrothermaux actifs
Editorial review for independent work. ICSAC — the Institute for Complexity
Science and Advanced Computing — runs a structured editorial panel for researchers
publishing outside journals, and publishes on CiteStamp rails. Submission is free
and goes through ORCID: icsacinstitute.org/submit.