Solvent accessible surface area (SASA) of proteins has always been considered as a
decisive factor in protein folding and stability studies. It is defined as the surface …

During the process of protein folding, the amino acid residues along the polypeptide chain
interact with each other in a cooperative manner to form the stable native structure. The …

The ability to predict local structural features of a protein from the primary sequence is of
paramount importance for unraveling its function in absence of experimental structural …

Motivation The accuracy of predicting protein local and global structural properties such as
secondary structure and solvent accessible surface area has been stagnant for many years …

Direct prediction of protein structure from sequence is a challenging problem. An effective
approach is to break it up into independent sub-problems. These sub-problems such as …

Protein secondary structure prediction began in 1951 when Pauling and Corey predicted
helical and sheet conformations for protein polypeptide backbone even before the first …

The relative solvent accessibility (RSA) of a residue in a protein measures the extent of
burial or exposure of that residue in the 3D structure. RSA is frequently used to describe a …

Background Estimation of the reliability of specific real value predictions is nontrivial and the
efficacy of this is often questionable. It is important to know if you can trust a given prediction …

Background Predicting 3-dimensional protein structures from amino-acid sequences is an
important unsolved problem in computational structural biology. The problem becomes …

Predicting one-dimensional structure properties has played an important role to improve
prediction of protein three-dimensional structures and functions. The most commonly …