Publisher Summary The comparison of protein sequences and structures is a critical first
step for a wide range of tasks that include, for example, the identification of related proteins …

A simple method of predicting residue solvent accessibilities in proteins is described, with
the intention that it should be used as a baseline by which more sophisticated approaches to …

We present a new method for protein secondary structure prediction, based on the
recognition of well-defined pentapeptides, in a large databank. Using a databank of 635 …

The deep-learning protein structure prediction method AlphaFold2 has garnered enormous
attention beyond the realm of structural biology, for its groundbreaking contribution to …

An easy and uncomplicated method to predict the solvent accessibility state of a site in a
multiple protein sequence alignment is described. The approach is based on amino acid …

A protein's amino acid sequence dictates the folds and final structure the macromolecule will
form. We propose that by identifying critical residues in a protein's atomic structure, we can …

A number of genetic diseases are a result of missense mutations in protein structure. These
mutations can lead to severe protein destabilization and misfolding. The unfolding mutation …

An increasing number of proteins with weak sequence similarity have been found to assume
similar three-dimensional fold and often have similar or related biochemical or biophysical …

Antibiotic resistance is a global concern. Two members of the bacterial genus
Elizabethkingia, namely, E. anophelis and E. meningoseptica have raised much concern in …

Rational design in protein engineering leads to significant progresses in medicinal
chemistry research. It alleviates the difficulty of exploring unreasonable biological functions …