Koder, Ronald 照片

Koder, Ronald

Associate Professor

所属大学: The City University of New York, CUNY

所属学院: Department of Chemistry

邮箱:
koder@sci.ccny.cuny.edu

个人主页:
http://web.sci.ccny.cuny.edu/~koder/koder.html

个人简介

Ph.D., The Johns Hopkins University; PostDoc, The University of Pennsylvania

研究领域

Molecular Biophysics

Methods, Artificial Blood, Protein Chemotherapeutics, and Solar Energy

近期论文

Mutter, A.C., Norman, J.C., Tiederman, M.T., Singh, S., Stillman, M.J., Koder, R.L.. Rational Design of a Zinc Phthalocyanine Binding Protein.(2013) J. Struct. Biol. In Press

Brown, M.C., Mutter, A.C., Koder, R.L., JiJi, R.D., Cooley, J.W. Direct quantification of persistent α-helical content and discrete types of backbone disorder during a molten globule to ordered peptide transition. (2013) J. Raman Spect. 44:957-962

Brisendine, J.M., Mutter, A.C., Cerda, J.F., Koder, R.L. A 3D Printed Cell for Rapid, Low Volume Spectroelectrochemistry. (2013) Anal. Biochem. 439:1-3

Zhang, L., Andersen, E.M.E., Khajo, A., Magliozzo, R.S., Koder, R.L. Dynamic Factors Affecting Gaseous Ligand Binding in an Artificial Oxygen Transport Protein. (2013) Biochemistry 52:447−455

Punnoose, A., McConnell, L., Liu, W., Mutter, A.C., Koder, R.L. Fundamental Limits on Wavelength, Efficiency and Yield of the Charge Separation Triad. (2012) PLOS One 7:e36065

Raju, G., Capo, J., Lichtenstein, B.R., Cerda, J.F., Koder, R.L. Manipulating reduction potentials in an artificial safranin cofactor. (2012) Tetrahedron Letters 53:1201–1203

Annavarapu, S., Zhang, L., Koder, R.L., Nanda, V. Computational Design of Thermostabilizing D-Amino Acid Substitutions. (2011) J. Amer. Chem. Soc. 133:18750–18759

Zhang, L., Anderson, J.L.R., Ahmed, I., Norman, J.A., Negron, C., Mutter, A.C., Dutton, P.L., Koder R.L. Manipulating Heme Binding Thermodynamics in an Artificial Oxygen Transport Protein. (2011) Biochemistry 50:10254–10261

Cui, D, Koder, R.L., Dutton, P.L., Miller, A.-F., 15N Solid-State NMR as a Probe of Flavin Hydrogen Bonding. (2011) J. Phys. Chem. B 115:7788–7798

Braun, P., Goldberg, E., Negron, C., von Jan, M, Xu, F., Nanda, V., Koder, R.L., Noy, D. Design Principles for Chlorophyll Binding Sites in Helical Proteins. (2011) Prot. Struct. Func. Bioinform. 79:463-476

Xu, F., Zhang, L., Koder, R.L., Nanda, V. De novo self-assembling collagen heterotrimers using explicit positive and negative design (2010) Biochemistry 49:2307-2316

Nanda, V. and Koder, R.L. Designing enzymes, from intuition to computation (2010) Nature Chemistry 2:15-24

Koder R.L.,* Anderson, R.,* Soloman, L.A., Reddy, K.S., Moser, C.M., Dutton, P.L. Design and engineering of an O(2) transport protein (2009) Nature 458:305-309 From Eric Drexler's Blog: Metamodern. A Revolution in de novo Protein Engineering Methodology. 2009.

Negron, C., Fufezan, C., Koder, R.L. Geometric constraints for porphyrin binding in helical protein binding sites (2009) Prot. Struct. Func. Bioinform. 74:400-416

Lichtenstein, B.R., Cerda, J.F., Koder, R.L., Dutton, P.L. Reversible Proton Coupled Electron Transfer in a Peptide-Incorporated Naphthoquinone Amino Acid (2009) Chem. Comm. 2:168-170

Anderson, R., Moser, C.M., Koder, R.L., Dutton, P.L. Controlling complexity and water penetration in functional de novo protein design (2008) Biochem. Soc. Trans. 36:1106-1111

Cerda, J.F., Koder, R.L., Lichtenstein, B.R., Moser, C.M., Miller, A.-F., Dutton, P.L. Hydrogen Bond-Free Flavin Redox Properties: Managing Flavins in Extreme Aprotic Solvents (2008) Org. & Biomol. Chem. 6:2204-2212

Koder, R.L.,Lichtenstein, B.R., Cerda, J.F., Miller, A.-F., Dutton, P.L. A flavin analogue with improved solubility in organic solvents (2007) Tetrahedron Letters 48: 5517-5520

Koder, R. L., Walsh, J. D., Pometun, M. S., Dutton, P. L., Wittebort, R. J., Miller, A.-F. 15N Solid-State NMR Provides a Sensitive Probe of Oxidized Flavin Reactive Sites (2006) J. Amer. Chem. Soc. 128: 15200-15208

Koder, R.L., Valentine, K. G., Cerda, J., Noy, D., Smith, K. M., Wand, A. J., Dutton, P. L. Nativelike Structure in Designed Four-Helix Bundles Driven by Buried Polar Interactions (2006) J. Amer. Chem. Soc. 128: 14450-14451