个人简介

Michael Hecht was born and grew up in midtown Manhattan. He received his BA in Chemistry from Cornell University, where he did undergraduate research on protein folding with Prof. Harold Scheraga. He completed his Ph.D. in Biology at MIT, where he received the first Ph.D. from Prof. Bob Sauer's lab, and did research on protein stability and protein/DNA interactions. He did post-doctoral research on protein design in the labs of Profs. David and Jane Richardson in the Biochemistry Department at Duke University Medical School. In 1990, Hecht joined the faculty of the Chemistry Department at Princeton, where he also holds an affiliated appointment in the Department of Molecular Biology. At Princeton, Hecht has served as the Director of Undergraduate Studies and Associate Chair of the Chemistry Department. In addition to his 'day job' in the Chemistry Department, Hecht is also the Master of Forbes College, one of the 6 undergraduate Colleges at Princeton (www.princeton.edu/forbescollege). When not in Frick or Forbes, he spends time traveling, skiing, inline skating, bicycling, and backpacking. The picture at right was taken in the Arctic National Wildlife Range in Northern Alaska.

研究领域

Synthetic biology: from protein design to artificial genomes/and Alzheimer's disease: molecular underpinnings and the search for new therapeutics.

Research in the Hecht group focuses in two areas: Synthetic Biology and Alzheimer's Disease. Although these fields may seem quite different, they explore two facets of the same problem. Synthetic biology requires an ability to devise novel proteins, which ultimately comes down to designing amino acid sequences that fold into a specific 3-dimensional structure. Conversely, probing the molecular underpinnings of Alzheimer’s disease requires an understanding of how sequences fail to fold into globular protein structures, but instead misfold into oligomeric or fibrillar structures.

近期论文

查看导师新发文章 （温馨提示：请注意重名现象，建议点开原文通过作者单位确认）

Smith BA, Mularz AM and MH Hecht (2014) Divergent evolution of a bifunctional de novo protein. Protein Science (24):246-252. Patel SC and MH Hecht (2012) Directed evolution of the peroxidase activity of a de novo-designed protein. Protein Engineering Design & Selection, online June 3, 2012 Cherny I, Korolev M, Koehler AN and MH Hecht (2012) Proteins from an Unevolved Library of de novo Designed Sequences Bind a Range of Small Molecules. ACS Synthetic Biology, 1, 130-138. Arai R, Kobayashi N, Kimura A, Sato T, Matsuo K, Wang AF, Platt JM, Bradley LH and MH Hecht (2012) Domain-Swapped Dimeric structure of a Stable and Functional De Novo Four-Helix Bundle Protein, WA20. Journal of Physical Chemistry B. Smith BA & Hecht MH (2011) Functional de novo Proteins (Review). Current Opinion in Chemical Biology., 15, 421–426. Das A, Wei Y, Pelczer I & Hecht MH (2011) Binding of small molecules to cavity forming mutants of de novo designed protein. Protein Science (20):702-711. Fisher MA, McKinley KL, Bradley LH, Viola SR & Hecht MH (2011) De Novo Designed Proteins From a Library of Artificial Sequences Function in Escherichia Coli and Enable Cell Growth. PLoS ONE 6(1): e15364. Patel S, Bradley LH, Jinadasa S, Hecht MH. (2009) Cofactor Binding and Enzymatic Activity in an Unevolved Superfamily of De Novo Designed 4-Helix Bundle Proteins. Protein Science 18, 1388-1400. Go A, Kim S, Baum J, & Hecht MH (2008) Structure and Dynamics of De novo Proteins from a Designed Superfamily of 4-Helix Bundles. Protein Science 17, 4. Das A, Hecht MH (2007) Peroxidase Activity of De Novo Heme Proteins Immobilized on Electrodes. J. Inorganic Biochemistry 101, 1820-1826. Das A, Trammell SA, & Hecht MH (2006) Electrochemical and ligand binding studies of a de novo heme protein. Biophysical Chemistry 123,102-112. Bradley LH, Thumfort P, Hecht MH. (2006) De Novo Proteins from Binary Patterned Combinatorial Libraries. Chapter 3 in Protein Design: Methods & Applications in Methods in Molecular Biology (Humana Press) 340, 53-69. Hu Y, Das A, Hecht MH & Scoles G (2005) Nanografting De Novo Proteins onto Gold Surfaces. Langmuir 21,9103-9109. Bradley LH, Kleiner RE, Wang AF, Hecht MH & Wood DW (2005) An Intein-Based Genetic Selection Enables Construction of a High-Quality Library of Binary Patterned De Novo Sequences. Protein Engineering, Design and Selection 18, 201-207. Klepeis JL, Wei Y, Hecht MH & Floudas CA (2004) Ab Initio Prediction of the 3-Dimensional Structure of a De Novo Designed Protein: A Double Blind Case Study. Proteins: Structure, Function, and Bioinformatics 58, 560-570. Hecht MH, Das A, Go A, Bradley LH, Wei Y (2004) De Novo Proteins From Designed Combinatorial Libraries.Protein Science 13, 1711-1723. Wei Y & Hecht MH (2004) Enzyme-like Proteins From an Unselected Library of Designed Amino Acid Sequences. Protein Engineering, Design and Selection 17, 67-75. Wei Y, Kim S, Fela D, Baum J, & Hecht MH (2003) Solution Structure of a De Novo Protein From a Designed Combinatorial Library. Proc. Natl. Acad. Sci. (USA) 100, 13270-13273. Moffet DA, Foley J, & Hecht MH (2003) Midpoint Reduction Potentials and Heme Binding Stoichiometries of De Novo Proteins from Designed Combinatorial Libraries. Biophysical Chemistry 105, 231-239. Wei Y, Liu T, Sazinsky SL, Moffet DA, Pelczer I, & Hecht MH (2003) Stably Folded De Novo Proteins From a Designed Combinatorial Library. Protein Science 12, 92-102.