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HORI - Introduction:
HORI - Higher Order Residue Interactions, is a web server to compute higher order interactions (pairwise interaction, triplet interactions and quadruple interactions) in a protein structure. HORI Server is available in three modules : HORI - Global, HORI - Lite and HORI - Cluster


HORI - Modules:

HORI - Global offers a set of algorithms to compute Pairwise, Triplet and Quadruple interactions among the residues in a protein structure. Here, the complete set of all possible interactions in each category will be computed.
HORI - Lite offers a set of programs, where user can compute Pairwise, Triplet and Quadruple interactions within the protein structure by selecting specific residue number(s).
HORI - Cluster offers a set of programs, where user can compute Pairwise, Triplet and Quadruple interactions within the protein structure by selecting specific residue type(s).

HORI - Methodology:

HORI (Higher Order Residue Interactions in proteins) server offers a set programs classified in to 3 modules as HORI – Global, HORI – Lite and HORI – Cluster for the analysis of protein structures. HORI server has been designed as an interactive, multiple module server for the computation of all possible higher order residue interactions in protein structures of single chain and higher oligomer structures with two chains. HORI offers enormous possibilities to understand details about higher order residue interaction with in protein structures in atomic level. HORI uses a set of distance based algorithms to compute higher order residue interactions in a protein structure. The interactions can be calculated based on C-&alpha and C-&beta atoms.


References:
  • Betancourt, M. R., Thirumalai, D. (1999). Pair potentials for protein folding: choice of reference states and sensitivity of predicted native states to variations in the interaction schemes. Protein Sci. 8, 361-369.
  • A. Godzik, A. Kolinski, and J. Skolnick. (1992) A topology fingerprint approach to inverse protein folding problem. J. Mol. Biol., 227:227–238.
  • Hin Hark Gan, Alexander Tropsha, and Tamar Schlick. (2001) Lattice Protein Folding With Two and Four-Body Statistical Potentials. PROTEINS: Structure, Function, and Genetics 43:161–174.
  • Herráez, A.. 2006. Biomolecules in the computer. Jmol to the rescue. Biochem. Mol. Biol. Educ. 34: 255–261.
  • Sayle R.A., Milner-White E.J. RASMOL: biomolecular graphics for all. Trends Biochem. Sci. 1995;20:374.
HORI Server is powered by : PDB, GNU C Compiler, JMol, RasMol, Apache, JScript & Perl
HORI Server can be accessed using different browsers, but we recommend : Mozilla Firefox (Windows/Linux) and Apple Safari (Mac)

Contact:
Prof. R. Sowdhamini (mini@ncbs.res.in)
HORI Server Team : P. Sundaramurthy, Raashi Sreenivasan, K. Shameer, Prof. Sunita Gakkhar & Prof. R. Sowdhamini