- University of Cologne, Cologne, Germany Vordiplom, 1972 in Chemistry, Physics
- University of Cologne, Cologne, Germany Diplom (MS), 1975 in Chemistry
- University of Cologne, Cologne, Germany Dr.rer.nat. (PhD), 1978, summa cum laude, in Organic Chemistry
- National Institute for Medical Research, Mill Hill, London Division of Molecular Pharmacology, Post Doc Advisor: James Feeney
Education & Training
Clore GM, Gronenborn AM. Structures of larger proteins in solution: three- and four-dimensional heteronuclear NMR spectroscopy. Science 252, 1390 (1991).
Frank MK, Dyda F, Dobrodumov A, Gronenborn AM. Core mutations switch monomeric protein GB1 into an intertwined tetramer. Nat. Struct. Biol., 9(11): 877-885 (2002).
Byeon, IL, Meng X, Jung J, Zhao G, Yang R, Ahn J, Shi J, Concel J, Aiken C, Zhang P, Gronenborn AM. Structural convergence between Cryo-EM and NMR reveals intersubunit interactions critical for HIV-1 capsid function. Cell 139, 780 (2009).
Koharudin LM, Liu L, Gronenborn AM. Different 3D domain-swapped oligomeric cyanovirin-N structures suggest trapped folding intermediates. Proc Natl Acad Sci U S A 110(19):7702-7 (2013).
Zhao G, Perilla JR, Yufenyuy EL, Meng X, Chen B, Ning J, Ahn J, Gronenborn AM, Schulten K, Aiken C, Zhang P. Mature HIV-1 capsid structure by cryo-electron microscopy and all-atom molecular dynamics. Nature 497(7451):643-646 (2013).
Matei E, Gronenborn AM. (19) F Paramagnetic relaxation enhancement: A valuable tool for distance measurements in proteins. Angew Chem Int Ed Engl 55(1) (2016).
Mitchell SD, Gronenborn AM. After 50 years, why are protein X-ray crystallographers still in business? Br J Philos Sci. 68: 703-723 (2017).
Byeon IL, Calero G, Wu Y, Byeon CH, Jung J, DeLucia M, Zhou X, Weiss S, Ahn J, Hao C, Skowronski J, Gronenborn AM. Structure of HIV-1 Vpr in complex with the human nucleotide excision repair protein hHR23A. Nat Commun. 25;12(1):6864 (2021).
Gronenborn AM. Small, but powerful and attractive: 19F in biomolecular NMR. Structure 30(1):6-14 (2022).
Zhu W, Yang DT, Gronenborn AM. Ligand-Capped Cobalt(II) Multiplies the Value of the Double-Histidine Motif for PCS NMR Studies. J Am Chem Soc. 145(8):4564-4569 (2023).
Bai XC, Gonen T, Gronenborn AM, Perrakis A, Thorn A, Yang J. Challenges and opportunities in macromolecular structure determination. Nat Rev Mol Cell Biol. 25(1):7-12 (2024).
In order to understand how biological macromolecules work and to intervene with respect to activity and function, detailed knowledge of their architecture and dynamic features is required. Characterizing the major determinants for stability and conformational specificity of normal and disease-causing forms of important molecules allows one to unravel the complex processes associated with disease. Angela Gronenborn's research combines nuclear magnetic resonance (NMR) spectroscopy and other structural techniques with biophysics, biochemistry, and chemistry in an integrative fashion to investigate cellular processes at the molecular and atomic levels in relation to human disease. Within her group, NMR methods for determining three-dimensional structures of biological macromolecules are developed and applied to challenging systems. Over the years, the Gronenborn group has solved structures of a large number of medically and biologically important proteins and protein complexes, such as various HIV and AIDS related proteins.
Molecular, Cellular and Behavioral Impact of the R203W PACS1 Syndrome Mutation
05/1/22 to 03/31/27
National Institutes of Health
R01
University of Pittsburgh Center for HIV Protein Interactions (PCHPI)
07/01/22 to 4/30/27
National Institutes of Health
U54
NSF/MCB-BSF The virtues of lanthanides and fluorine for tracking in-cell protein conformation: a marriage of NMR and EPR
06/01/21 to 05/31/25
National Science Foundation
Structural Characterization of SARS-CoV-2 Genome Organization by NMR
04/1/23 to 03/31/26
National Science Foundation