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Chemistry

D-Index
56
Citations
12080
World Ranking
11556
National Ranking
3121

Research.com Recognitions

  • 2003 - Fellow of the American Association for the Advancement of Science (AAAS)

Overview

Erik R. P. Zuiderweg is affiliated with the University of Michigan-Ann Arbor in the United States. Their research primarily spans biochemistry, genetics, molecular biology, and chemistry, with a focus on molecular biology and spectroscopy.

Their recent publications cover various aspects of protein dynamics and nuclear magnetic resonance (NMR) techniques. Notable papers include:

  • New experimental evidence for pervasive dynamics in proteins (2023, Protein Science)
  • Simulating the Motion Underlying the Mechanism of Thioredoxin Reductase (2024, ACS Omega)
  • Multispin Cross-Correlated Transverse Dipolar NMR Relaxation in Solution (2022, Concepts in Magnetic Resonance Part A)
  • Hommage to Richard R. Ernst (2021, Frontiers in Molecular Biosciences)
  • Validating the 15N-1H HSQC-ROESY experiment for detecting 1HN exchange broadening in proteated proteins (2024, Journal of Magnetic Resonance)

Their scientific work addresses topics such as protein structure and dynamics, advanced NMR techniques and applications, and NMR spectroscopy and applications. Additional research areas include mass spectrometry techniques, lipid membrane structure and behavior, redox biology and oxidative stress, and metal-catalyzed oxygenation mechanisms.

Frequent co-authors in their publications include David A. Case, Charles H. Williams, Anja Böckmann, Rachel W. Martin, and Ann E. McDermott. The research output has appeared in several venues, notable among which are Protein Science, ACS Omega, Concepts in Magnetic Resonance Part A, Frontiers in Molecular Biosciences, and the Journal of Magnetic Resonance.

Zuiderweg's contributions to the academic community are recognized in part by their fellowship with the American Association for the Advancement of Science (AAAS), awarded in 2003.

Best Publications

  • The role of dynamics in allosteric regulation.

    Dorothee Kern;Erik R P Zuiderweg

  • Mapping protein-protein interactions in solution by NMR spectroscopy.

    Erik R. P. Zuiderweg

  • Heteronuclear three-dimensional nmr spectroscopy. A strategy for the simplification of homonuclear two-dimensional NMR spectra

    Stephen W Fesik;Erik R.P Zuiderweg

  • A protein structure from nuclear magnetic resonance data. Lac Repressor headpiece

    R. Kaptein;E.R.P. Zuiderweg;R.M. Scheek;R. Boelens

  • Solution conformation of wild-type E. coli Hsp70 (DnaK) chaperone complexed with ADP and substrate.

    Eric B. Bertelsen;Lyra Chang;Jason E. Gestwicki;Erik R. P. Zuiderweg

  • Heteronuclear three-dimensional NMR spectroscopy of the inflammatory protein C5a

    Erik R. P. Zuiderweg;Stephen W. Fesik

  • Chemical Manipulation of Hsp70 ATPase Activity Regulates Tau Stability

    Umesh K. Jinwal;Yoshinari Miyata;John Koren;Jeffrey R. Jones

  • Structural insights into substrate binding by the molecular chaperone DnaK.

    M Pellecchia;D L Montgomery;D L Montgomery;S Y Stevens;C W Vander Kooi

  • 2D and 3D NMR spectroscopy employing carbon-13/carbon-13 magnetization transfer by isotropic mixing. Spin system identification in large proteins

    Stephen W. Fesik;Hugh L. Eaton;Edward T. Olejniczak;Erik R. P. Zuiderweg

  • Allosteric drugs: the interaction of antitumor compound MKT-077 with human Hsp70 chaperones.

    Aikaterini Rousaki;Yoshinari Miyata;Umesh K. Jinwal;Chad A. Dickey

  • Allostery in the Hsp70 chaperone proteins.

    Erik R. P. Zuiderweg;Eric B. Bertelsen;Aikaterini Rousaki;Aikaterini Rousaki;Matthias P. Mayer

  • High-throughput screen for small molecules that modulate the ATPase activity of the molecular chaperone DnaK.

    Lyra Chang;Eric B. Bertelsen;Susanne Wisén;Erik M. Larsen

  • High-resolution solution structure of the 18 kDa substrate-binding domain of the mammalian chaperone protein Hsc70.

    Robert C Morshauser;Weidong Hu;Hong Wang;Yuxi Pang

  • PROTEIN NMR RELAXATION : THEORY, APPLICATIONS AND OUTLOOK

    Mark W.F. Fischer;Ananya Majumdar;Erik R.P. Zuiderweg

  • Binding of a small molecule at a protein-protein interface regulates the chaperone activity of hsp70-hsp40.

    Susanne Wisén;Eric B Bertelsen;Andrea D Thompson;Srikanth Patury

  • Analogues of the Allosteric Heat Shock Protein 70 (Hsp70) Inhibitor, MKT-077, As Anti-Cancer Agents

    Xiaokai Li;Sharan R. Srinivasan;Jamie Connarn;Atta Ahmad

  • Improvement of 2D NOE spectra of biomacromolecules in H2O solution by coherent suppression of the solvent resonance

    Erik R.P Zuiderweg;Klaas Hallenga;Edward T Olejniczak

  • Heat shock protein 70 kDa chaperone/DnaJ cochaperone complex employs an unusual dynamic interface

    Atta Ahmad;Akash Bhattacharya;Akash Bhattacharya;Ramsay A. McDonald;Melissa Cordes

  • Two-dimensional double quantum 1H NMR spectroscopy of proteins.

    Gerhard Wagner;Erik R.P. Zuiderweg

  • The solution structure of the bacterial HSP70 chaperone protein domain DnaK(393-507) in complex with the peptide NRLLLTG.

    Shawn Y. Stevens;Sheng Cai;Maurizio Pellecchia;Erik R.P. Zuiderweg

  • Three-dimensional 13C-resolved proton NOE spectroscopy of uniformly 13C-labeled proteins for the NMR assignment and structure determination of larger molecules

    Erik R.P Zuiderweg;Lawrence P McIntosh;Frederick W Dahlquist;Stephen W Fesik

Frequent Co-Authors

Jason E. Gestwicki
Jason E. Gestwicki University of California, San Francisco
Maurizio Pellecchia
Maurizio Pellecchia University of California, Riverside
Stephen W. Fesik
Stephen W. Fesik Vanderbilt University
Gary D. Glick
Gary D. Glick University of Michigan–Ann Arbor
Chad A. Dickey
Chad A. Dickey University of South Florida
Stephen W. Ragsdale
Stephen W. Ragsdale University of Michigan–Ann Arbor
Gabor Tigyi
Gabor Tigyi University of Tennessee Health Science Center
Franco Quadrifoglio
Franco Quadrifoglio University of Udine
Dietmar J. Manstein
Dietmar J. Manstein Hannover Medical School
Christoph Schick
Christoph Schick University of Rostock

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