This article contains inter-residue solvent accessible surface distances between lysines in a comprehensive dataset homo-oligomeric protein complex structures, downloaded from 3D Complex database. Solvent Accessible Surface Distances were calculated with Jwalk algorithm. To avoid unnecessary redundancy due to symmetry, we calculated only distances originating from the first subunit of each protein complex. Redundancy was further reduced by including only the shortest of the two possible inter-subunit alternatives in the final non-redundant dataset. For each protein complexes we also calculated weight ob subunits, number of lysines radius of gyration and average distances. This data can be used for structural analyses of homo-oligomeric pro...
<div><p>Chemical cross-linking/Mass Spectrometry (XLMS) is an experimental method to obtain distance...
Background: Distance geometry methods allow protein structures to be constructed using a large numbe...
Prediction of protein structures from sequences and protein-protein interaction from structures are ...
The three-dimensional structures of proteins are stabilized by the interactions between amino acid r...
The analysis of amino acid coevolution has emerged as a practical method for protein structural mode...
Motivation: Chemical cross-linking of proteins or protein complexes and the mass spectrometry based ...
The prediction of protein structures is a current issue of great significance in structural bioinfor...
Cellular processes often depend on interactions between proteins and the formation of macromolecular...
ABSTRACT Protein solvation energies are of-ten taken to be proportional to solvent-accessible surfac...
The ab initio prediction of a protein's 3D-structure from its amino acid sequence remains an un...
BackgoundUnknown protein structures can be predicted from known structures (the scaffolds) with sequ...
Abstract Background Depending on chemical features residues have preferred locations – interior or e...
Distances measured between distinctive parts of amino acid residues surrounding the ligand
This is the publisher's version, also available electronically from "http://peds.oxfordjournals.org"...
Motivation: Chemical cross-linking/mass spectrometry (XLMS) is an experimental method to obtain dist...
<div><p>Chemical cross-linking/Mass Spectrometry (XLMS) is an experimental method to obtain distance...
Background: Distance geometry methods allow protein structures to be constructed using a large numbe...
Prediction of protein structures from sequences and protein-protein interaction from structures are ...
The three-dimensional structures of proteins are stabilized by the interactions between amino acid r...
The analysis of amino acid coevolution has emerged as a practical method for protein structural mode...
Motivation: Chemical cross-linking of proteins or protein complexes and the mass spectrometry based ...
The prediction of protein structures is a current issue of great significance in structural bioinfor...
Cellular processes often depend on interactions between proteins and the formation of macromolecular...
ABSTRACT Protein solvation energies are of-ten taken to be proportional to solvent-accessible surfac...
The ab initio prediction of a protein's 3D-structure from its amino acid sequence remains an un...
BackgoundUnknown protein structures can be predicted from known structures (the scaffolds) with sequ...
Abstract Background Depending on chemical features residues have preferred locations – interior or e...
Distances measured between distinctive parts of amino acid residues surrounding the ligand
This is the publisher's version, also available electronically from "http://peds.oxfordjournals.org"...
Motivation: Chemical cross-linking/mass spectrometry (XLMS) is an experimental method to obtain dist...
<div><p>Chemical cross-linking/Mass Spectrometry (XLMS) is an experimental method to obtain distance...
Background: Distance geometry methods allow protein structures to be constructed using a large numbe...
Prediction of protein structures from sequences and protein-protein interaction from structures are ...