Many efforts were spent in the last years in bridging the gap between the huge number of sequenced proteins and the relatively few solved structures. Relative Solvent Accessibility (RSA) prediction of residues in protein complexes is a key step towards secondary structure and protein-protein interaction sites prediction. With very different approaches, a number of software tools for RSA prediction have been produced throughout the last twenty years. Here, we present a binary classifier which implements a new method mainly based on sequence homology and implemented by means of look-up tables. The tool exploits residue similarity in solvent exposure pattern of neighboring context in similar protein chains, using BLAST search and DSSP structur...
An easy and uncomplicated method to predict the solvent accessibility state of a site in a multiple ...
Residue depth (RD) is a solvent exposure measure that complements the information provided by conven...
Background : Structural properties of proteins such as secondary structure and solvent accessibilit...
Many efforts were spent in the last years in bridging the gap between the huge number of sequenced p...
Residue solvent accessibility is closely related to the spatial arrangement and packing of residues....
A working example of relative solvent accessibility (RSA) prediction for proteins is presented. Nove...
Characterization of relative solvent accessibility (RSA) plays a major role in classifying a given p...
Abstract Background Prediction of protein solvent accessibility, also called accessible surface area...
Prediction of protein structures from sequences and protein-protein interaction from structures are ...
[[abstract]]In this thesis, I investigated how the amino acids physicochemical environment informati...
Proteins have vital roles in the living cells. The protein function is almost completely dependent o...
Predicting the three-dimensional structure of proteins is a long-standing challenge of computational...
Residue depth (RD) is a solvent exposure measure that complements the information provided by conven...
[[abstract]]We investigate how residue structural and physicochemical environment information, such ...
Motivation: The prediction of ligand-binding residues or catalytically active residues of a protein ...
An easy and uncomplicated method to predict the solvent accessibility state of a site in a multiple ...
Residue depth (RD) is a solvent exposure measure that complements the information provided by conven...
Background : Structural properties of proteins such as secondary structure and solvent accessibilit...
Many efforts were spent in the last years in bridging the gap between the huge number of sequenced p...
Residue solvent accessibility is closely related to the spatial arrangement and packing of residues....
A working example of relative solvent accessibility (RSA) prediction for proteins is presented. Nove...
Characterization of relative solvent accessibility (RSA) plays a major role in classifying a given p...
Abstract Background Prediction of protein solvent accessibility, also called accessible surface area...
Prediction of protein structures from sequences and protein-protein interaction from structures are ...
[[abstract]]In this thesis, I investigated how the amino acids physicochemical environment informati...
Proteins have vital roles in the living cells. The protein function is almost completely dependent o...
Predicting the three-dimensional structure of proteins is a long-standing challenge of computational...
Residue depth (RD) is a solvent exposure measure that complements the information provided by conven...
[[abstract]]We investigate how residue structural and physicochemical environment information, such ...
Motivation: The prediction of ligand-binding residues or catalytically active residues of a protein ...
An easy and uncomplicated method to predict the solvent accessibility state of a site in a multiple ...
Residue depth (RD) is a solvent exposure measure that complements the information provided by conven...
Background : Structural properties of proteins such as secondary structure and solvent accessibilit...