Homme Wytzes Hellinga

About

Homme Wytzes Hellinga is the James B. Duke Distinguished Professor of Biochemistry and a Professor of Biochemistry at Duke University. He is a primary faculty member in the Duke Department of Biochemistry, working within the Hellinga Lab. His research focuses on biochemistry, and he is involved in teaching and mentoring within the department. His contact email is hwh@biochem.duke.edu, and he is based at 413D Nanaline H Duke, Research Drive, Durham, NC 27708.

Research topics

• Biology
• Computer Science
• Chemistry
• Artificial Intelligence
• Computational chemistry
• Statistical physics
• Physics
• Biological system
• Biochemistry
• Microbiology

Selected publications

• Structural evidence for the rare tautomer hypothesis of spontaneous mutagenesis

  Proceedings of the National Academy of Sciences · 2011-10-17 · 263 citations

  article

  Even though high-fidelity polymerases copy DNA with remarkable accuracy, some base-pair mismatches are incorporated at low frequency, leading to spontaneous mutagenesis. Using high-resolution X-ray crystallographic analysis of a DNA polymerase that catalyzes replication in crystals, we observe that a C • A mismatch can mimic the shape of cognate base pairs at the site of incorporation. This shape mimicry enables the mismatch to evade the error detection mechanisms of the polymerase, which would…

  PublisherDOI

• Structures of Human Exonuclease 1 DNA Complexes Suggest a Unified Mechanism for Nuclease Family

  Cell · 2011-04-01 · 162 citations

  articleOpen access
  PublisherOA PDFDOI

• Thermodynamic Analysis of Ligand-Induced Changes in Protein Thermal Unfolding Applied to High-Throughput Determination of Ligand Affinities with Extrinsic Fluorescent Dyes

  Biochemistry · 2010-11-04 · 116 citations

  articleOpen accessSenior author

  The quantification of protein-ligand interactions is essential for systems biology, drug discovery, and bioengineering. Ligand-induced changes in protein thermal stability provide a general, quantifiable signature of binding and may be monitored with dyes such as Sypro Orange (SO), which increase their fluorescence emission intensities upon interaction with the unfolded protein. This method is an experimentally straightforward, economical, and high-throughput approach for observing thermal melts…

  PublisherOA PDFDOI

• Multifactorial Determinants of Protein Expression in Prokaryotic Open Reading Frames

  Journal of Molecular Biology · 2010-08-19 · 107 citations

  articleSenior authorCorresponding
  PublisherDOI

• Quantitation of protein–protein interactions by thermal stability shift analysis

  Protein Science · 2011-06-14 · 74 citations

  articleOpen accessSenior authorCorresponding

  Thermal stability shift analysis is a powerful method for examining binding interactions in proteins. We demonstrate that under certain circumstances, protein-protein interactions can be quantitated by monitoring shifts in thermal stability using thermodynamic models and data analysis methods presented in this work. This method relies on the determination of protein stabilities from thermal unfolding experiments using fluorescent dyes such as SYPRO Orange that report on protein denaturation. Dat…

  PublisherOA PDFDOI

Recent grants

• NIH Grant R29GM049871

  NIH · $534k · 1999

• NIH Grant R01GM049871

  NIH · $2.3M · 2008

• NIH Grant DP1OD000122

  NIH · $3.8M · 2010

Frequent coauthors

• L.S. Beese

  Duke University Hospital

  57 shared

• John P. Caradonna

  Boston University

  43 shared

• Malin Allert

  Duke Medical Center

  38 shared

• Loren L. Looger

  36 shared

• M.J. Cuneo

  St. Jude Children's Research Hospital

  27 shared

• Wei Yang

  Hunan University of Science and Engineering

  27 shared

• Jenny J. Yang

  Georgia State University

  27 shared

• Yiming Ye

  Key Laboratory of Guangdong Province

  25 shared

Education

• Ph.D., Biochemistry

  University of Groningen

  1976

• M.S., Biochemistry

  University of Groningen

  1973

• B.S., Biochemistry

  University of Groningen

  1971

Similar researchers at Duke University

• Robert J. Lefkowitzh-328
• Paul Modrichh-148
• Patrick John Caseyh-109