World's Best Scientists 2026 revealed!

D-Index & Metrics

Chemistry

D-Index
60
Citations
14141
World Ranking
9623
National Ranking
2704

Overview

Michael H. Hecht is affiliated with Princeton University in the United States and conducts research primarily within the broad domain of Biochemistry, Genetics and Molecular Biology. Their work spans several interrelated subfields, including Molecular Biology, Materials Chemistry, Biotechnology, Biomedical Engineering, and Ecology.

The scientist's research portfolio covers key topics such as Protein Structure and Dynamics, Chemical Synthesis and Analysis, Enzyme Structure and Function, Quantum Dots Synthesis and Properties, Nanocluster Synthesis and Applications, Enzyme Production and Characterization, and Innovative Microfluidic and Catalytic Techniques Innovation.

Michael H. Hecht has contributed to numerous publications characterized by frequent appearances in prominent scientific journals. These include:

  • Biopolymers
  • Proceedings of the National Academy of Sciences
  • Journal of the American Chemical Society
  • Nature Chemistry
  • Life

Recent scholarly articles associated with this researcher demonstrate a focus on protein design and synthetic biology applications. Selected papers include:

  • "A Completely De Novo ATPase from Combinatorial Protein Design" (2020), published in the Journal of the American Chemical Society
  • "A Strategy for Combinatorial Cavity Design in De Novo Proteins" (2020), published in Life
  • "A de novo protein catalyzes the synthesis of semiconductor quantum dots" (2022), published in Proceedings of the National Academy of Sciences
  • "Selection of a promiscuous minimalist cAMP phosphodiesterase from a library of de novo designed proteins" (2024), published in Nature Chemistry
  • "Harnessing synthetic biology to enhance heterologous protein expression" (2020), published in Protein Science

Collaboration forms a significant aspect of their scientific activity. Frequent co-authors include:

  • Elkan Blout
  • Murray Goodman
  • Ephraim Katchalski
  • David N. Beratan
  • Stephen C. Blacklow

Best Publications

  • Protein design by binary patterning of polar and nonpolar amino acids

    Satwik Kamtekar;Jarad M. Schiffer;Jarad M. Schiffer;Huayu Xiong;Jennifer M. Babik

  • Amyloid-like Aggregates Sequester Numerous Metastable Proteins with Essential Cellular Functions

    Heidi Olzscha;Sonya M. Schermann;Andreas C. Woerner;Stefan Pinkert

  • De novo design, expression, and characterization of Felix: a four-helix bundle protein of native-like sequence

    Michael H. Hecht;Jane S. Richardson;David C. Richardson;Richard C. Ogden

  • De novo amyloid proteins from designed combinatorial libraries.

    Michael W. West;Weixun Wang;Jennifer Patterson;Joseph D. Mancias

  • Periodicity of polar and nonpolar amino acids is the major determinant of secondary structure in self-assembling oligomeric peptides.

    Huayu Xiong;Brian L. Buckwalter;Hong-Ming Shieh;Michael H. Hecht

  • Mutations that Reduce Aggregation of the Alzheimer's Aβ42 Peptide: an Unbiased Search for the Sequence Determinants of Aβ Amyloidogenesis

    Christine Wurth;Nathalie K Guimard;Michael H Hecht

  • Recombinant Proteins Can Be Isolated from E. coli Cells by Repeated Cycles of Freezing and Thawing

    Brian H. Johnson;Michael H. Hecht

  • De novo proteins from designed combinatorial libraries.

    Michael H. Hecht;Aditi Das;Abigail Go;Luke H. Bradley

  • Generic hydrophobic residues are sufficient to promote aggregation of the Alzheimer's Aβ42 peptide

    Woojin Kim;Michael H. Hecht

  • A High-Throughput Screen for Compounds That Inhibit Aggregation of the Alzheimer's Peptide

    Woojin Kim;Yunkyoung Kim;Jaeki Min;Dong Jin Kim

  • Nature disfavors sequences of alternating polar and non-polar amino acids: implications for amyloidogenesis.

    Bede M. Broome;Michael H. Hecht

  • Rationally designed mutations convert de novo amyloid-like fibrils into monomeric β-sheet proteins

    Weixun Wang;Michael H. Hecht

  • Binary patterning of polar and nonpolar amino acids in the sequences and structures of native proteins

    Michael W. West;Michael H. Hecht

  • Mutations in lambda repressor's amino-terminal domain: implications for protein stability and DNA binding

    Michael H. Hecht;Hillary C. M. Nelson;Robert T. Sauer

  • Sequence determinants of enhanced amyloidogenicity of Alzheimer Aβ42 peptide relative to Aβ40

    Woojin Kim;Michael H. Hecht

  • Solution structure of a de novo protein from a designed combinatorial library.

    Yinan Wei;Seho Kim;David Fela;Jean Baum

  • Protein Design: The Choice of de Novo Sequences *

    James R. Beasley;Michael H. Hecht

  • Stabilization of λ repressor against thermal denaturation by site‐directed Gly→Ala changes in α‐helix 3

    Michael H. Hecht;Julian M. Sturtevant;Robert T. Sauer

  • De novo proteins from combinatorial libraries.

    David A. Moffet;Michael H. Hecht

  • A novel inhibitor of amyloid β (Aβ) peptide aggregation: from high throughput screening to efficacy in an animal model of Alzheimer disease.

    Angela Fortner McKoy;Jermont Chen;Trudi Schupbach;Michael H. Hecht

  • Stably folded de novo proteins from a designed combinatorial library

    Yinan Wei;Tun Liu;Stephen L. Sazinsky;David A. Moffet

Frequent Co-Authors

Thomas G. Spiro
Thomas G. Spiro University of Washington
Jean Baum
Jean Baum Rutgers, The State University of New Jersey
Young-Tae Chang
Young-Tae Chang Pohang University of Science and Technology
Trudi Schüpbach
Trudi Schüpbach Princeton University
George McLendon
George McLendon Princeton University
John T. Groves
John T. Groves Princeton University
Giacinto Scoles
Giacinto Scoles University of Udine
Manajit Hayer-Hartl
Manajit Hayer-Hartl Max Planck Society
Takeshi Fukuma
Takeshi Fukuma Kanazawa University
Ilhan A. Aksay
Ilhan A. Aksay Princeton University

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