Isaac A. Hubner, PhD, is a Technology Specialist in the Patent Law and Life Sciences Practice Groups of Proskauer Rose LLP. His practice encompasses all aspects of obtaining and enforcing clients’ intellectual property rights in the US and abroad. Dr. Hubner is registered to practice before the US Patent and Trademark Office and is a 2009 JD candidate at Suffolk University.

Dr. Hubner earned his PhD in physical chemistry from Harvard University, where he was a Howard Hughes Medical Institute Fellow. While at Harvard University, Dr. Hubner conducted research with Prof. Eugene I. Shakhnovich in computational biology. In particular, Dr. Hubner’s research focused on the development and implementation of atomic-resolution models of protein structure and dynamics. His research extended into the fields of bioinformatics, protein engineering, drug design, and human disease. Dr. Hubner also holds an AM in chemistry from Harvard University and BS in biochemistry, magna cum laude and Phi Beta Kappa, from the University of Delaware.

At Proskauer, Dr. Hubner works closely with clients in the biotechnology and high-technology industries. He has experience in medical and industrial biotechnology (e.g., protein nucleic acid engineering and biofuels), pharmaceuticals and therapeutics (e.g., cancer, HIV/AIDS, antimicrobials and drug formulation), medical devices (e.g., surgical and cosmetic lasers, drug delivery systems, wound care and diagnostics) and materials and manufacturing (e.g., ceramic composites, solar cells, optical storage media, automobiles and semiconductors).

Dr. Hubner has published numerous peer-reviewed articles, which include the following:

Understanding ensemble protein folding at atomic detail by Hubner IA, Deeds EJ, Shakhnovich EI PNAS 103:47 17747-17752 (NOV 21, 2006)

Common motifs and topological effects in the protein folding transition state by Hubner IA, Lindberg M, Haglund E, et al. J MOL BIO 359:4 1075-1085 (JUN 16, 2006)

Identification of the minimal protein-folding nucleus through loop-entropy perturbations by Lindberg MO, Haglund E, Hubner IA, et al. PNAS 103:11 4083-4088 (MAR 14, 2006)

On the origin and highly likely completeness of single-domain protein structures by Zhang Y, Hubner IA, Arakaki AK, et al. PNAS 103:8 2605-2610 (FEB 21, 2006)

High-resolution protein folding with a transferable potential by Hubner IA, Deeds EJ, Shakhnovich EI PNAS 102:52 18914-18919 (DEC 27, 2005)

Geometric and physical considerations for realistic protein models by Hubner IA, Shakhnovich EI PHYS REV E 72:2 Article Number 022901(AUG 2005)

Nucleation and the transition state of the SH3 domain by Hubner IA, Edmonds KA, Shakhnovich EI J MOL BIO 349:2 424-434 (JUN 3, 2005)

Mutant-selective thyromimetics for the chemical rescue of thyroid hormone receptor mutants associated with resistance to thyroid hormone by Shi Y, Ye H, Link KH, Putnam MC, Hubner I, Dowdell S, Koh JT BIOCHEMSITRY 44:12 4612-26 (MAR 29, 2005)

CoC: a database of universally conserved residues in protein folds by Donald JE, Hubner IA, Rotemberg VM, et al. BIOINFORMATICS 21:10 2539-2540 (MAY 15, 2005)

Simulation, experiment, and evolution: Understanding nucleation in protein S6 folding by Hubner IA, Oliveberg M, Shakhnovich EI PNAS 101:22 8354-8359 (JUN 1, 2004)

Commitment and nucleation in the protein G transition state by Hubner IA, Shimada J, Shakhnovich EI J MOL BIO 336:3 745-761 (FEB 20, 2004)

X-ray photoelectron spectroscopy of nitromethane adsorption products on Si(100): A model for N1s core-level shifts in silicon oxynitride films by Eng J, Hubner IA, Barriocanal J, et al. J APPLIED PHYS 95:4 1963-1968 (FEB 15, 2004)