Dr. Gerig received his Ph.D. from Brown University and spent two years doing postdoctoral research at the California Institute of Technology before joining the UCSB faculty in 1966. He has been a PHS Research Career Development Awardee and is a Fellow of the AAAS and the Japan Association for the Promotion of Science. He retired in 2006 but remains active in his research.
Addition of small molecules, such as an alcohol or an osmolyte, to aqueous solutions of peptides and proteins often alters the dominant conformation of these biomaterials. Why these effects occur is not always apparent, although at least in some cases it appears that selective interaction of the biomolecule with the small molecules is involved. Over the past few years, we have used heteronuclear and homonuclear intermolecular NOE experiments to examine such solvent-biopolymer interactions.
Interpretation of these NOE experiments can be done using a model of the system of interest that treats all molecules as hard spheres. This approach can produce predictions that agree with experimental results; unusual solvent-solute interactions are indicated when such agreement is absent. It is challenging to develop understanding of any solvent-solute system at the molecular level when the hard spheres model fails. We are, thus, developing all-atom molecular dynamics (MD) simulations of the systems of interest to aid in interpretation of experimental results previously reported from our lab.
Current efforts are focused on an analog of the peptide hormone angiotensin II, the mini-protein Trp-cage and melittin, a component of bee venom. Conformation-altering small molecules under study include various hydrocarbon and fluorocarbon alcohols and the osmolyte trimethylamine N-oxide (TMAO).
Selected Research Publications
J. T. Gerig, Examination of trifluoroethanol interactions with Trp-Cage in trifluoroethanol-water at 298 K through MD simulations and intermolecular nuclear Overhauser effects, J Phys. Chem. B (2019), in press.
J. T. Gerig, Examination of ethanol interactions with Trp-cage peptide through MD simulations and intermolecular nuclear Overhauser effects, J. Phys. Org. Chem. (2018); e3809. https://doi.org/10.1002/poc.3809.
J. T. Gerig, Examination of trifluoroethanol interactions with Trp-cage through MD simulations and intermolecular nuclear Overhauser effects, J. Phys. Chem. B 120 (2016), 11256-11265.
J. T. Gerig, Further efforts toward a molecular dynamics force field for simulations of peptides in 40% trifluoroethanol-water, J. Phys. Chem. B 119 (2015), 5163-5175.
J. T. Gerig, Toward a molecular dynamics force field for simulations of 40% trifluoroethanol-water, J. Phys. Chem. B. 118 (2014), 1471-1480.
J. T. Gerig, Investigation of ethanol-peptide and water-peptide interactions through intermolecular NOEs and molecular dynamics simulations, J. Phys. Chem. B 117 (2013), 4880-4892.
J. T. Gerig, Investigation of methanol-peptide nuclear Overhauser effects through molecular dynamics simulations, J. Phys. Chem. B 116 (2012), 1965-1973.
J. T. Gerig, Nuclear spin relaxation in liquid acetonitrile, Mol. Sim. 38 (2011), 1085-1093.
R. C. Neuman, Jr., J. T. Gerig, Interactions of nonprotic organic solvents with [val5]angiotensin in water, J. Phys. Chem. B 115 (2011),1712-1719.
J. T. Gerig,, Cross relaxation in liquid methanol, J. Magn. Reson. 210 (2011), 171-176.
Y. Suzuki, T. Asakura, J. T. Gerig, NMR study of interactions between a silk model peptide and fluorinated alcohols for preparation of regenerated silk fiber, Macromolecules 43 (2010), 2364-2370.
R. C. Neuman, Jr., J. T. Gerig, Interaction of alcohols with [Val5]angiotensin in alcohol-water mixtures, J. Phys. Chem. B 114 (2010), 6722-6731.
D. P. Chagolla, J. T. Gerig, Conformations of Betanova in aqueous trifluoroethanol, Biopolymers 93 (2010), 893-903.