Protein kinetic stability
JM Sanchez-Ruiz - Biophysical chemistry, 2010 - Elsevier
The relevance of protein stability for biological function and molecular evolution is widely
recognized. Protein stability, however, comes in two flavours: thermodynamic stability, which …
recognized. Protein stability, however, comes in two flavours: thermodynamic stability, which …
Improvement of microbial α-amylase stability: strategic approaches
TB Dey, A Kumar, R Banerjee, P Chandna… - Process …, 2016 - Elsevier
Microbial α-amylase being a vital enzyme in industrial biotechnology, has also received
enormous attention in academic field. Although a huge number of α-amylases from different …
enormous attention in academic field. Although a huge number of α-amylases from different …
Structural basis of homo-and heterotrimerization of collagen I
Fibrillar collagen molecules are synthesized as precursors, procollagens, with large
propeptide extensions. While a homotrimeric form (three α1 chains) has been reported in …
propeptide extensions. While a homotrimeric form (three α1 chains) has been reported in …
Thermal, chemical and pH induced denaturation of a multimeric β-galactosidase reveals multiple unfolding pathways
Background In this case study, we analysed the properties of unfolded states and pathways
leading to complete denaturation of a multimeric chick pea β-galactosidase (Cp GAL), as …
leading to complete denaturation of a multimeric chick pea β-galactosidase (Cp GAL), as …
How aggregation and conformational scrambling of unfolded states govern fluorescence emission spectra
In a case study on five homologous α-amylases we analyzed the properties of unfolded
states as obtained from treatments with GndHCl and with elevated temperatures. In …
states as obtained from treatments with GndHCl and with elevated temperatures. In …
Temperature stability of proteins: Analysis of irreversible denaturation using isothermal calorimetry
A Schön, BR Clarkson, M Jaime… - … : Structure, Function, and …, 2017 - Wiley Online Library
The structural stability of proteins has been traditionally studied under conditions in which
the folding/unfolding reaction is reversible, since thermodynamic parameters can only be …
the folding/unfolding reaction is reversible, since thermodynamic parameters can only be …
Thermostable bacterial laccase: catalytic properties and its application in biotransformation of emerging pollutants
Laccases have been predominantly reported in fungi, and primarily, fungal laccases are
currently exploited in industrial applications. However, extremophilic bacterial laccases …
currently exploited in industrial applications. However, extremophilic bacterial laccases …
Biovalorisation of mixed food waste through newly isolated thermo tolerant fungal cell factories: A step toward transforming waste to wealth
Food waste is a lucrative biomass consisting of abundant complex organic content that can
be reduced to simpler compounds and channelled towards bio-manufacturing. In this study …
be reduced to simpler compounds and channelled towards bio-manufacturing. In this study …
Protein adsorption to charged gold nanospheres as a function of protein deformability
The corona that forms as protein adsorbs to gold nanospheres (AuNSs) is directly influenced
by the surface chemistry of the AuNS. Tools to predict adsorption outcomes are needed for …
by the surface chemistry of the AuNS. Tools to predict adsorption outcomes are needed for …
The evolution of cyclodextrin glucanotransferase product specificity
Cyclodextrin glucanotransferases (CGTases) have attracted major interest from industry due
to their unique capacity of forming large quantities of cyclic α-(1, 4)-linked oligosaccharides …
to their unique capacity of forming large quantities of cyclic α-(1, 4)-linked oligosaccharides …