Difference between revisions of "WHAT IF"
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'''WHAT IF''' is a computer program used in a wide variety of 'in silico'' macromolecular structure research fields such as: | '''WHAT IF''' is a computer program used in a wide variety of 'in silico'' macromolecular structure research fields such as: | ||
| − | *homology models of protein tertiary structures as well as quaternary structures; | + | *[[Homology modeling|homology models]] of protein tertiary structures as well as quaternary structures; |
*validation of protein structures, noticeably those deposited in the [[PDB]]; | *validation of protein structures, noticeably those deposited in the [[PDB]]; | ||
*correction of protein structures; | *correction of protein structures; | ||
| − | *visualisation of macromolecules and their interaction partners (lipids, | + | *visualisation of macromolecules and their interaction partners (lipids, drugs, ions, water); and |
*interactive manipulation of macromolecules | *interactive manipulation of macromolecules | ||
Its best known use has been the detection of many millions (often small, but sometimes catastrophic) [http://swift.cmbi.ru.nl/gv/pdbreport/ errors] in PDB files. | Its best known use has been the detection of many millions (often small, but sometimes catastrophic) [http://swift.cmbi.ru.nl/gv/pdbreport/ errors] in PDB files. | ||
| + | |||
| + | ==See also== | ||
| + | *[[wikipedia:Category:Molecular modelling software]] | ||
| + | *[http://biskit.pasteur.fr/ Biskit] — written in [[Python]] | ||
| + | *[http://noch.sourceforge.net/ NOCH] (or NOC) | ||
| + | *[[Jmol]] | ||
| + | *[[PyMOL]] | ||
| + | *[[RasMol]] | ||
| + | *[[Homology modeling]] | ||
==References== | ==References== | ||
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* Nabuurs SB, Spronk CA, Vuister GW, Vriend G. (2006) Traditional biomolecular structure determination by NMR spectroscopy allows for major errors. ''PLoS Comput. Biol.'' 2, e9. | * Nabuurs SB, Spronk CA, Vuister GW, Vriend G. (2006) Traditional biomolecular structure determination by NMR spectroscopy allows for major errors. ''PLoS Comput. Biol.'' 2, e9. | ||
</div> | </div> | ||
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==External links== | ==External links== | ||
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[[Category:Bioinformatics]] | [[Category:Bioinformatics]] | ||
| + | [[Category:Crystallography]] | ||
Latest revision as of 00:05, 13 July 2012
WHAT IF is a computer program used in a wide variety of 'in silico macromolecular structure research fields such as:
- homology models of protein tertiary structures as well as quaternary structures;
- validation of protein structures, noticeably those deposited in the PDB;
- correction of protein structures;
- visualisation of macromolecules and their interaction partners (lipids, drugs, ions, water); and
- interactive manipulation of macromolecules
Its best known use has been the detection of many millions (often small, but sometimes catastrophic) errors in PDB files.
See also
- wikipedia:Category:Molecular modelling software
- Biskit — written in Python
- NOCH (or NOC)
- Jmol
- PyMOL
- RasMol
- Homology modeling
References
- G. Vriend, (1990). WHAT IF: A molecular modeling and drug design program. J. Mol. Graph. 8, 52-56.
- G. Vriend, (1990). Parameter relation rows: a query system for protein structure function relationships. Prot. Engin. 4, 221-223.
- G. Vriend, C. Sander, (1991). Detection of common three-dimensional substructures in proteins. PROTEINS 11, 52-58.
- G. Vriend, C. Sander. (1993). Quality control of protein models: Directional atomic contact analysis. J. Appl. Cryst. 26, 47-60.
- V. de Filippis, C. Sander, G. Vriend, (1994). Predicting local structural changes that result from point mutations. Prot. Engin. 7, 1203-1208.
- G. Vriend, C. Sander, P.F.W. Stouten, (1994). A novel search method for protein sequence-structure relations, using property profiles. Prot. Engin. 7, 23-29.
- R. Hooft, C. Sander, G. Vriend, (1994). Reconstruction of symmetry related molecules from protein data bank (PDB) files. J. Appl. Cryst. 27, 1006-1009.
- G. Chinea, G. Padron, R.W.W.Hooft, C.Sander, G.Vriend, (1995). The use of position specific rotamers in model building by homology. PROTEINS 23, 415-421.
- R.W.W.Hooft, C.Sander, G.Vriend, (1996). Positioning hydrogen atoms by optimizing hydrogen-bond networks in protein structures. PROTEINS 26, 363-376.
- R.W.W. Hooft, G. Vriend, C. Sander, E.E. Abola, (1996). Errors in protein structures. Nature 381, 272-272.
- R.W.W. Hooft, C.Sander and G.Vriend, (1996). Verification of protein structures: Side-chain planarity. J. Appl. Cryst. 29, 714--716.
- R.W.W. Hooft, C.Sander and G.Vriend, (1997). Objectively judging the quality of a protein structure from a Ramachandran plot. CABIOS (Now: Bioinformatics) 13, 425-430.
- K.Wilson, C.Sander, R.W.W.Hooft, G.Vriend, et al., (1998). Who checks the checkers? Four validation tools applied to eight atomic resolution structures. J. Mol. Biol. 276,417-436.
- R.Rodriguez, G.Chinea, N.Lopez, T.Pons, G.Vriend, (1998). Homollogy modelling, model and software evaluation: three related resources. Bioinformatics 14, 523-528.
- J.E. Nielsen, K.V. Andersen, B. Honig, R.W. Hooft, G. Klebe, G. Vriend, R.C. Wade, (1999). Improving macromolecular electrostatics calculations. Prot. Engin. 12, 657-662.
- Rodriguez R, Chinea G, Lopez N, Vriend G, (1999) Full window stereo. J. Mol. Graph. & Mod. 17, 310-313.
- Altenberg-Greulich, B., Vriend G., (2001) Where to attach dye molecules to a protein: lessons from WHAT IF. J. Mol. Struc. 598, 1-8.
- Nielsen, JE., Vriend G. (2001) Optimizing the Hydrogen-Bond Network in Poisson-Boltzmann Equation-based pKa Calculations. PROTEINS 43, 403-412.
- Nabuurs SB, Spronk CA, Krieger E, Maassen H, Vriend G, Vuister GW. (2003) Quantitative evaluation of experimental NMR restraints. JACS 2003 125, 12026-12034.
- Spronk CA, Nabuurs SB, Bonvin AM, Krieger E, Vuister GW, Vriend G., (2003) The precision of NMR structure ensembles revisited. J. Biomol. NMR 25, 225-234.
- Krieger E, Nabuurs SB, Vriend G. (2003) Homology modeling. Methods Biochem. Anal. 44, 509-523.
- Nabuurs SB, Spronk CA, Vuister GW, Vriend G. (2006) Traditional biomolecular structure determination by NMR spectroscopy allows for major errors. PLoS Comput. Biol. 2, e9.
