Polar hydrogen positions in proteins: empirical energy placement and neutron diffraction comparison. Export

@article{brunger:88, abstract = {A method for the prediction of hydrogen positions in proteins is presented. The method is based on the knowledge of the heavy atom positions obtained, for instance, from X-ray crystallography. It employs an energy minimization limited to the environment of the hydrogen atoms bound to a common heavy atom or to a single water molecule. The method is not restricted to proteins and can be applied without modification to nonpolar hydrogens and to nucleic acids. The method has been applied to the neutron diffraction structures of trypsin, ribonuclease A, and bovine pancreatic trypsin inhibitor. A comparison of the constructed and the observed hydrogen positions shows few deviations except in situations in which several energetically similar conformations are possible. Analysis of the potential energy of rotation of Lys amino and Ser, Thr, Tyr hydroxyl groups reveals that the conformations of lowest intrinsic torsion energies are statistically favored in both the crystal and the constructed structures.}, author = {Br\"{u}nger, A. T. and Karplus, M.}, citeulike-article-id = {3865583}, citeulike-linkout-0 = {http://dx.doi.org/10.1002/prot.340040208}, citeulike-linkout-1 = {http://view.ncbi.nlm.nih.gov/pubmed/3227015}, citeulike-linkout-2 = {http://www.hubmed.org/display.cgi?uids=3227015}, doi = {10.1002/prot.340040208}, issn = {0887-3585}, journal = {Proteins}, keywords = {interactions, protonation, software}, number = {2}, pages = {148--156}, posted-at = {2009-01-08 22:59:43}, priority = {0}, title = {Polar hydrogen positions in proteins: empirical energy placement and neutron diffraction comparison.}, url = {http://dx.doi.org/10.1002/prot.340040208}, volume = {4}, year = {1988} }

TY - JOUR ID - brunger:88 L3 - citeulike-article-id:3865583 N2 - A method for the prediction of hydrogen positions in proteins is presented. The method is based on the knowledge of the heavy atom positions obtained, for instance, from X-ray crystallography. It employs an energy minimization limited to the environment of the hydrogen atoms bound to a common heavy atom or to a single water molecule. The method is not restricted to proteins and can be applied without modification to nonpolar hydrogens and to nucleic acids. The method has been applied to the neutron diffraction structures of trypsin, ribonuclease A, and bovine pancreatic trypsin inhibitor. A comparison of the constructed and the observed hydrogen positions shows few deviations except in situations in which several energetically similar conformations are possible. Analysis of the potential energy of rotation of Lys amino and Ser, Thr, Tyr hydroxyl groups reveals that the conformations of lowest intrinsic torsion energies are statistically favored in both the crystal and the constructed structures. IS - 2 JF - Proteins SN - 0887-3585 EP - 156 TI - Polar hydrogen positions in proteins: empirical energy placement and neutron diffraction comparison. VL - 4 SP - 148 KW - interactions KW - protonation KW - software AU - Brünger, AT AU - Karplus, M PY - 1988/// UR - http://dx.doi.org/10.1002/prot.340040208 ER -