The amino acid sequence of a protein affects both its structure and its function. Thus, the
ability to modify the sequence, and hence the structure and activity, of individual proteins in …

Maintaining the structure of protein and peptide drugs has become one of the most important
goals of scientists in recent decades. Cold and thermal denaturation conditions …

The interactions of biological macromolecules with water are fundamental to their structure,
dynamics and function. Historically, characterization of the location and residence times of …

Thermostable enzymes that hydrolyze lignocellulosic materials provide potential
advantages in process configuration and enhancement of production efficiency over their …

The shape of the protein surface dictates what interactions are possible with other
macromolecules, but defining discrete pockets or possible interaction sites remains difficult …

An entropic stabilization mechanism has recently gained attention and credibility as the
physical ground for the extra thermal stability of globular proteins from thermophilic …

Carbonic anhydrase can be used as an additive to improve the efficiency of carbon capture
and utilisation processes, due to its ability to increase the rate of CO 2 absorption into …

Encapsulation of small molecules, proteins, and other macromolecules within the protective
water core of reverse micelles is emerging as a powerful strategy for a variety of …

Infections caused by multidrug-resistant pathogens are one of the biggest challenges facing
the healthcare system today. Quorum quenching (QQ) enzymes have the potential to be …

Background: Ferritin has an important role in iron storage in the cells, and due to its
nanocage structure and self-assembly properties, it has wide application prospects in …