His primary areas of investigation include Crystallography, Dipole, Peptide, Nuclear magnetic resonance spectroscopy and Solid-state nuclear magnetic resonance. His research in Crystallography intersects with topics in Side chain, Molecular recognition, Adsorption and Protein secondary structure. His research integrates issues of Spectral line, Molecular physics, Spins, Computational chemistry and Nuclear magnetic resonance in his study of Dipole.
Magnetic dipole–dipole interaction is closely connected to Amino acid in his research, which is encompassed under the umbrella topic of Peptide. His Nuclear magnetic resonance spectroscopy research is multidisciplinary, relying on both Computational physics and Molecule. His work carried out in the field of Solid-state nuclear magnetic resonance brings together such families of science as Infrared spectroscopy, Analytical chemistry and Dynamics.
Gary P. Drobny mainly investigates Crystallography, Solid-state nuclear magnetic resonance, Nuclear magnetic resonance spectroscopy, Nuclear magnetic resonance and Peptide. His Crystallography research includes elements of Deuterium NMR, Protein secondary structure, Molecular recognition, Adsorption and Side chain. His Solid-state nuclear magnetic resonance study also includes fields such as
His research investigates the connection between Nuclear magnetic resonance spectroscopy and topics such as Relaxation that intersect with problems in Residual dipolar coupling. His Nuclear magnetic resonance study combines topics in areas such as Spectral line, Molecular physics and Spectroscopy. His Spectral line research focuses on Molecule and how it connects with Computational chemistry.
His main research concerns Peptide, Crystallography, Solid-state nuclear magnetic resonance, Molecular dynamics and Nuclear magnetic resonance spectroscopy. His Peptide study incorporates themes from Nanotechnology, Precipitation, Biophysics, Lysine and Protein structure. The various areas that Gary P. Drobny examines in his Crystallography study include Amino acid, Deuterium NMR, Deuterium, Magic angle spinning and Side chain.
His work deals with themes such as Protein secondary structure, Two-dimensional nuclear magnetic resonance spectroscopy, Biomineralization, Spectral line and Tar, which intersect with Solid-state nuclear magnetic resonance. Gary P. Drobny does research in Nuclear magnetic resonance spectroscopy, focusing on Residual dipolar coupling specifically. Relaxation is the subject of his research, which falls under Nuclear magnetic resonance.
Gary P. Drobny focuses on Peptide, Amino acid, Biophysics, Nanotechnology and Solid-state nuclear magnetic resonance. The study incorporates disciplines such as Precipitation, Biomolecule, Lysine, Folding and Phosphorylation in addition to Peptide. His Lysine research incorporates elements of Turn, Helix and Protein secondary structure.
His Amino acid research includes themes of Crystallography, Side chain, Prebiotic and Fatty acid. His Biophysics research integrates issues from Molecular recognition, Peptide Conformation and Molecular dynamics. His studies deal with areas such as Crystallization and Tar as well as Solid-state nuclear magnetic resonance.
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Assignment of the non-exchangeable proton resonances of d(C-G-C-G-A-A-T-T-C-G-C-G) using two-dimensional nuclear magnetic resonance methods.
Dennis R. Hare;David E. Wemmer;Shan-Ho Chou;Gary Drobny.
Journal of Molecular Biology (1983)
Fourier transform multiple quantum nuclear magnetic resonance
Gary Drobny;Alexander Pines;Steven Sinton;Daniel P. Weitekamp.
Faraday Symposia of The Chemical Society (1978)
Optimization of two-dimensional homonuclear relayed coherence transfer NMR spectroscopy
Ad Bax;Gary Drobny.
Journal of Magnetic Resonance (1985)
Solution Structure of a Cisplatin-Induced DNA Interstrand Cross-Link
Huifang Huang;Leiming Zhu;Brian R. Reid;Gary P. Drobny.
The Amide 15N Chemical Shift Tensors of Four Peptides Determined from 13C Dipole-Coupled Chemical Shift Powder Patterns
Terrence G. Oas;Cynthia J. Hartzell;Frederick W. Dahlquist;Gary P. Drobny.
Journal of the American Chemical Society (1987)
Determination of the nitrogen-15 and carbon-13 chemical shift tensors of L-[13C]alanyl-L-[15N]alanine from the dipole-coupled powder patterns
C. J. Hartzell;M. Whitfield;T. G. Oas;G. P. Drobny.
Journal of the American Chemical Society (1987)
Structure and Dynamics of Hydrated Statherin on Hydroxyapatite As Determined by Solid-State NMR†
Joanna R. Long;Wendy J. Shaw;Patrick S. Stayton;Gary P. Drobny.
Windowless dipolar recoupling: the detection of weak dipolar couplings between spin 12 nuclei with large chemical shift anisotropies
D.M. Gregory;D.J. Mitchell;J.A. Stringer;S. Kiihne.
Chemical Physics Letters (1995)
Chimeric peptides of statherin and osteopontin that bind hydroxyapatite and mediate cell adhesion.
Michele Gilbert;Wendy J. Shaw;Joanna R. Long;Kjell E. Nelson.
Journal of Biological Chemistry (2000)
Molecular Recognition at the Protein-Hydroxyapatite Interface
Patrick S. Stayton;Gary P. Drobny;Wendy J. Shaw;Joanna R. Long.
Critical Reviews in Oral Biology & Medicine (2003)
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