Charged and polar groups, through forming ion pairs, hydrogen bonds, and other less
specific electrostatic interactions, impart important properties to proteins. Modulation of the …

Natural proteins are often only slightly more stable in the native state than the denatured
state, and an increase in environmental temperature can easily shift the balance toward …

A central feature of the SARS-CoV-2 pandemic is that some individuals become severely ill
or die, whereas others have only a mild disease course or are asymptomatic. Here, we …

INTRODUCTION Temperature is crucially important to life. Small temperature changes can
differentiate optimal and lethal growth conditions of living organisms. Because of the higher …

The high temperature, acidity, and heavy metal-rich environments associated with hot
springs have a major impact on biological processes in resident cells. One group of …

Temperature profoundly influences physiological responses in animals, primarily due to the
effects on biochemical reaction rates. Since physiological responses are often exemplified …

The immobilization of proteins (mostly typically enzymes) onto solid supports is mature
technology and has been used successfully to enhance biocatalytic processes in a wide …

Protein function requires the folded protein form, but this form is unstable mainly because it
readily unfolds into a flexible, unstructured form. Protein folding is favored by burying of …

Lignocellulose is the most abundant carbohydrate source in nature and represents an ideal
renewable energy source. Thermostable enzymes that hydrolyze lignocellulose to its …

The molecular bases of thermal and cold stability and adaptation, which allow proteins to
remain folded and functional in the temperature ranges in which their host organisms live …