Structural Biology (Grzesiek)

Petrovic, Ivana, Grzesiek, Stephan and Isaikina, Polina (2024) ‘Advances in the molecular understanding of GPCR-arrestin complexes’, Biochemical Society Transactions, 52(6), pp. 2333–2342. Available at: https://doi.org/10.1042/BST20240170.

Petrovic, Ivana et al. (2024) ‘A high-resolution analysis of arrestin2 interactions responsible for CCR5 endocytosis’, bioRxiv [Preprint]. Cold Spring Harbor Laboratory (bioRxiv). Available at: https://doi.org/10.1101/2024.11.04.621860.

Hiller, Sebastian et al. (2024) ‘A functional chaperone condensate in the endoplasmic reticulum’, Research Square [Preprint]. Research Square (Research Square). Available at: https://doi.org/10.21203/rs.3.rs-4796355/v1.

Abiko, Layara Akemi et al. (2024) ‘Biased agonism of carvedilol in the beta1-adrenergic receptor is governed by conformational exclusion’, bioRxiv [Preprint]. Cold Spring Harbor Laboratory (bioRxiv). Available at: https://doi.org/10.1101/2024.07.19.604263.

Paladini, Johannes et al. (2024) ‘The molecular basis of Abelson kinase regulation by its αI-helix’, eLife, 12(Version of Record). Available at: https://doi.org/10.7554/elife.92324.3.

Hiller, Sebastian and Mas, Guillaume (2024) ‘Characterization of ATP hydrolysis in the Hsp70 BiP nucleotide binding domain’, Research Square [Preprint]. Research Square Platform LLC (Research Square). Available at: https://doi.org/10.21203/rs.3.rs-4017836/v1.

Cebrero Acuna, G.F. (2024) Structural and functional characterization of the teichoic acid flippase TacF from S. pneumoniae.

Petrovic, I. (2024) The molecular basis of the impact of GPCR phosphorylation on arrestin interactions and receptor endocytosis.

Paladini, Johannes et al. (2023) ‘The molecular basis of Abelson kinase regulation by its αI-helix’, eLife [Preprint]. Available at: https://doi.org/10.7554/elife.92324.

Paladini, J. et al. (2023) ‘The molecular basis of Abelson kinase regulation by its αI-helix’. bioRxiv. Available at: https://doi.org/10.1101/2023.10.04.560671.

Isaikina , P. (2023) Structural and functional analysis of the human chemokine receptor and HIV-1 co-receptor CCR5.

Isaikina, Polina et al. (2023) ‘A key GPCR phosphorylation motif discovered in arrestin2⋅CCR5 phosphopeptide complexes’, Molecular cell, 83(12), pp. 2108–2121.e7. Available at: https://doi.org/10.1016/j.molcel.2023.05.002.

Grzesiek, Stephan et al. (2022) ‘Imatinib disassembles the regulatory core of Abelson kinase by binding to its ATP site and not by binding to its myristoyl pocket’, Magnetic Resonance, (3), pp. 91–99. Available at: https://doi.org/10.5194/mr-2022-6.

Abiko, Layara Akemi et al. (2022) ‘Filling of a water-free void explains the allosteric regulation of the β1-adrenergic receptor by cholesterol’, Nature Chemistry, 14(10), pp. 1133–1141. Available at: https://doi.org/10.1038/s41557-022-01009-9.

Grzesiek, Stephan et al. (2022) ‘Imatinib disassembles the regulatory core of Abelson kinase by binding to its ATP site and not by binding to its myristoyl pocket’, Magnetic Resonance, 3, pp. 91–99. Available at: https://doi.org/10.5194/mr-3-91-2022.

Jahnke, Wolfgang et al. (2022) ‘Correspondence on ‘Synergy and Antagonism between Allosteric and Active-Site Inhibitors of Abl Tyrosine Kinase’’, Angewandte Chemie International Edition, 61(46), p. e202117276. Available at: https://doi.org/10.1002/anie.202117276.

Isaikina, Polina et al. (2022) ‘Preparation of a stable CCL5·CCR5·Gi signaling complex for Cryo-EM analysis’, in Shukla, Arun K. (ed.) Biomolecular Interactions Part B. Amsterdam, Netherlands: Elsevier (Methods in Cell Biology), pp. 115–141. Available at: https://doi.org/10.1016/bs.mcb.2022.03.001.

Abiko, Layara Akemi et al. (2021) ‘Filling of a water-free void explains the allosteric regulation of the β₁-adrenergic receptor by cholesterol’. bioRxiv. Available at: https://doi.org/10.1101/2021.08.30.457941.

Abiko, Layara Akemi et al. (2021) ‘Efficient production of a functional G protein-coupled receptor in E. coli for structural studies’, Journal of Biomolecular NMR, 75(1), pp. 25–38. Available at: https://doi.org/10.1007/s10858-020-00354-6.

Isaikina, Polina et al. (2021) ‘Structural basis of the activation of the CC chemokine receptor 5 by a chemokine agonist’, Science Advances, 7(25), p. eabg8685. Available at: https://doi.org/10.1126/sciadv.abg8685.

Schlotte, J. (2021) Investigation of the Abl regulatory core dynamics by single molecule FRET and solution NMR.

Franke, Bastian et al. (2020) ‘Versatile modules enable automated multi-column purifications on the ÄKTA pure chromatography system’, Journal of Chromatography A, 1618, p. 460846. Available at: https://doi.org/10.1016/j.chroma.2019.460846.

Grahl, Anne et al. (2020) ‘A high-resolution description of β1-adrenergic receptor functional dynamics and allosteric coupling from backbone NMR’, Nature communications, 11(1), p. 2216. Available at: https://doi.org/10.1038/s41467-020-15864-y.

Hee, Chee-Seng et al. (2020) ‘Intercepting second-messenger signaling by rationally designed peptides sequestering c-di-GMP’, Proceedings of the National Academy of Sciences of the United States of America, 117(29), pp. 17211–17220. Available at: https://doi.org/10.1073/pnas.2001232117.

Abiko, Layara Akemi, Grahl, Anne and Grzesiek, Stephan (2019) ‘High Pressure Shifts the β1-Adrenergic Receptor to the Active Conformation in the Absence of G Protein’, Journal of the American Chemical Society, 141(42), pp. 16663–16670. Available at: https://doi.org/10.1021/jacs.9b06042.

Opitz, Christian et al. (2019) ‘Deuterium induces a distinctive Escherichia coli proteome that correlates with the reduction in growth rate’, Journal of Biological Chemistry, 294(7), pp. 2279–2292. Available at: https://doi.org/10.1074/jbc.ra118.006914.

Opitz, Christian et al. (2019) ‘Rapid determination of general cell status, cell viability, and optimal harvest time in eukaryotic cell cultures by impedance flow cytometry’, Applied microbiology and biotechnology, 103(20), pp. 8619–8629. Available at: https://doi.org/10.1007/s00253-019-10046-3.

Franke, Bastian et al. (2018) ‘Production of isotope-labeled proteins in insect cells for NMR’, Journal of biomolecular NMR, 71(3), pp. 173–184. Available at: https://doi.org/10.1007/s10858-018-0172-7.

Grahl, A. (2018) NMR analysis of dynamics and interactions of two G protein-coupled receptors : the HIV-1 coreceptor CCR5 and the β1-adrenergic receptor. Available at: https://doi.org/10.5451/unibas-007198343.

Sonti, Rajesh et al. (2018) ‘ATP Site Ligands Determine the Assembly State of the Abelson Kinase Regulatory Core via the Activation Loop Conformation’, Journal of the American Chemical Society, 140(5), pp. 1863–1869. Available at: https://doi.org/10.1021/jacs.7b12430.

Delgado, L. (2017) Characterization of structure, dynamics and inter- actions of the lipopolysaccharide- binding protein LBP, the hepatitis B virus X protein (HBx) and the unfolded-state ensemble of ubiquitin. Available at: https://doi.org/10.5451/unibas-007085052.

Grzesiek, Stephan (2017) ‘Kann man die Biologie vorausberechnen?’, in Füglister, K. M.; Hicklin, M.; Mäser, P. (ed.) natura obscura. Basel: Schwabe AG (natura obscura), pp. 73–74.

Aznauryan, Mikayel et al. (2016) ‘Comprehensive structural and dynamical view of an unfolded protein from the combination of single-molecule FRET, NMR, and SAXS’, Proceedings of the National Academy of Sciences, 113(37), pp. E5389–98. Available at: https://doi.org/10.1073/pnas.1607193113.

Hoi Tik Alvin Leung et al. (2016) ‘A Rigorous and Efficient Method To Reweight Very Large Conformational Ensembles Using Average Experimental Data and To Determine Their Relative Information Content’, Journal of chemical theory and computation, 12(1), pp. 383–394. Available at: https://doi.org/10.1021/acs.jctc.5b00759.

Isogai, Shin et al. (2016) ‘Backbone NMR reveals allosteric signal transduction networks in the β1-adrenergic receptor’, Nature, 530(7589), pp. 237–41. Available at: https://doi.org/10.1038/nature16577.

Opitz, C. (2016) Development and application of an economic approach to isotope labeling in higher eukaryotes for NMR studies. Available at: https://doi.org/10.5451/unibas-006808759.

Bignucolo, Olivier et al. (2015) ‘Backbone hydration determines the folding signature of amino acid residues’, Journal of the American Chemical Society, 137(13), pp. 4300–3. Available at: https://doi.org/10.1021/jacs.5b00660.

Lamley, Jonathan M et al. (2015) ‘Unraveling the complexity of protein backbone dynamics with combined (13)C and (15)N solid-state NMR relaxation measurements’, Physical Chemistry, Chemical Physics, 17(34), pp. 21997–2008. Available at: https://doi.org/10.1039/c5cp03484a.

Opitz, Christian, Isogai, Shin and Grzesiek, Stephan (2015) ‘An economic approach to efficient isotope labeling in insect cells using homemade 15N-, 13C- and 2H-labeled yeast extracts’, Journal of Biomolecular NMR, 62(3), pp. 373–385. Available at: https://doi.org/10.1007/s10858-015-9954-3.

Habazettl, Judith et al. (2014) ‘Structural basis and dynamics of multidrug recognition in a minimal bacterial multidrug resistance system’, Proceedings of the National Academy of Sciences of the United States of America, 111(51), pp. E5498–507. Available at: https://doi.org/10.1073/pnas.1412070111.

Lamley, Jonathan M et al. (2014) ‘Solid-state NMR of a protein in a precipitated complex with a full-length antibody’, Journal of the American Chemical Society, 136(48), pp. 16800–6. Available at: https://doi.org/10.1021/ja5069992.

Bignucolo, Olivier, Grzesiek, Stephan and Bernèche, Simon (2013) ‘Aromatic Amino Acids Confer Folding Propensities to a Nine-Residue Peptide’, Biophysical Journal, 104(2), p. 400a. Available at: https://doi.org/10.1016/j.bpj.2012.11.2231.

Gentner, M. (2013) Folding of the transcription factor Brinker and interactions of the bacterial second messenger c-di-GMP studied by NMR. Available at: https://doi.org/10.5451/unibas-006089963.

Maciej, W. (2013) Towards NMR analysis of the HIV-1 coreceptor CCR5 and its interaction with RANTES. Available at: https://doi.org/10.5451/unibas-006202884.

Nielsen, Gerd et al. (2013) ‘Kinase in Motion : Insights into the Dynamic Nature of p38α by High-Pressure NMR Spectroscopic Studies’, ChemBioChem, 14(14), pp. 1799–806. Available at: https://doi.org/10.1002/cbic.201300170.

Ramón-García, Santiago et al. (2013) ‘WhiB7, an Fe-S-dependent Transcription Factor That Activates Species-specific Repertoires of Drug Resistance Determinants in Actinobacteria’, Journal of biological chemistry, 288(48), pp. 34514–28. Available at: https://doi.org/10.1074/jbc.m113.516385.

Skora, Lukasz et al. (2013) ‘NMR reveals the allosteric opening and closing of Abelson tyrosine kinase by ATP-site and myristoyl pocket inhibitors’, Proceedings of the National Academy of Sciences of the United States of America, 110(47), pp. E4437–45. Available at: https://doi.org/10.1073/pnas.1314712110.

Vajpai, Navratna et al. (2013) ‘High-pressure NMR reveals close similarity between cold and alcohol protein denaturation in ubiquitin’, Proceedings of the National Academy of Sciences of the United States of America, 110(5), pp. E368–76. Available at: https://doi.org/10.1073/pnas.1212222110.

Wiktor, Maciej, Hartley, Oliver and Grzesiek, Stephan (2013) ‘Characterization of Structure, Dynamics, and Detergent Interactions of the Anti-HIV Chemokine Variant 5P12-RANTES’, Biophysical journal, 105(11), pp. 2586–97. Available at: https://doi.org/10.1016/j.bpj.2013.10.025.

Wiktor, Maciej et al. (2013) ‘Biophysical and structural investigation of bacterially expressed and engineered CCR5, a G protein-coupled receptor.’, Journal of Biomolecular NMR, 55(1), pp. 79–95. Available at: https://doi.org/10.1007/s10858-012-9688-4.

Bax, Ad and Grzesiek, Stephan (2012) ‘ChemInform Abstract: ROESY’, ChemInform, 43(36). Available at: https://doi.org/10.1002/chin.201236274.

Huang, Jie-rong et al. (2012) ‘Sequence-Specific Mapping of the Interaction between Urea and Unfolded Ubiquitin from Ensemble Analysis of NMR and Small Angle Scattering Data’, Journal of the American Chemical Society, 134(9), pp. 4429–36. Available at: https://doi.org/10.1021/ja2118688.

Huang, Jie-rong et al. (2012) ‘Residual dipolar couplings measured in unfolded proteins are sensitive to amino-acid-specific geometries as well as local conformational sampling’, Biochemical Society transactions, 40(5), pp. 989–94. Available at: https://doi.org/10.1042/bst20120187.

Morin, Sébastien et al. (2012) ‘Interactions of CCR5, the Main HIV Coreceptor, with Rantes and Other Ligands’, in 56th Annual Meeting of the Biophysical-Society. San Diego, California (56th Annual Meeting of the Biophysical-Society), pp. 239a–240a. Available at: https://doi.org/10.1016/j.bpj.2011.11.1319.

Nisius, Lydia and Grzesiek, Stephan (2012) ‘Key stabilizing elements of protein structure identified through pressure and temperature perturbation of its hydrogen bond network’, Nature chemistry, 4(9), pp. 711–7. Available at: https://doi.org/10.1038/nchem.1396.

Secchi, Massimiliano et al. (2012) ‘Enhancement of Anti-HIV-1 Activity by Hot Spot Evolution of RANTES-Derived Peptides.’, Chemistry & Biology, 19(12), pp. 1579–88. Available at: https://doi.org/10.1016/j.chembiol.2012.10.007.

Van den Bergh, Rafael et al. (2012) ‘Monocytes Contribute to Differential Immune Pressure on R5 versus X4 HIV through the Adipocytokine Visfatin/NAMPT’, PLoS ONE, 7(4), p. e35074. Available at: https://doi.org/10.1371/journal.pone.0035074.

Vuister, G.W. et al. (2011) ‘Measurement of Structural Restraints’. John Wiley and Sons, pp. 83–157. Available at: https://doi.org/10.1002/9781119972006.ch4.

Bigalke, Janna M. et al. (2011) ‘Structure and Dynamics of a Stabilized Coiled-Coil Domain in the P-TEFb Regulator Hexim1’, Journal of Molecular Biology, 414(5), pp. 639–53. Available at: https://doi.org/10.1016/j.jmb.2011.10.022.

Dames, Sonja A. et al. (2011) ‘Structure, dynamics, lipid binding, and physiological relevance of the putative GTPase-binding domain of Dictyostelium formin C’, Journal of Biological Chemistry, 286(42), pp. 36907–20. Available at: https://doi.org/10.1074/jbc.m111.225052.

Habazettl, Judith et al. (2011) ‘Solution structure of the PilZ domain protein PA4608 complex with cyclic di-GMP identifies charge clustering as molecular readout’, Journal of biological chemistry, 286(16), pp. 14304–14. Available at: https://doi.org/10.1074/jbc.m110.209007.

Lewandowski, Józef R. et al. (2011) ‘Site-specific measurement of slow motions in proteins’, Journal of the American Chemical Society, 133(42), pp. 16762–5. Available at: https://doi.org/10.1021/ja206815h.

Nikolaev, Y. (2011) Rethinking Leucine Zipper : ribonuclease activity and structural dynamics of a ubiquitous oligomerization motif. Available at: https://doi.org/10.5451/unibas-005582107.

Grzesiek, Stephan and Becker, Edwin D. (2011) ‘Hydrogen bonding’, in Harris, Robin K.; Wasylishen, Roderick E. (ed.) Encyclopedia of NMR. Chichester: John Wiley (Encyclopedia of NMR), pp. 1929–1935. Available at: https://doi.org/10.1002/9780470034590.emrstm0216.pub2.

Vuister, Geerten W. et al. (2011) ‘Measurement of structural restraints in ‘A guide to protein NMR spectroscopy’’, in Lian, Lu-Yun; Roberts, Gordon (ed.) Protein NMR spectroscopy : principal techniques and applications. Chichester: John Wiley & Sons (Protein NMR spectroscopy : principal techniques and applications), p. S. 351.

Huang, Jie-rong and Grzesiek, Stephan (2010) ‘Ensemble calculations of unstructured proteins constrained by RDC and PRE data : a case study of urea-denatured ubiquitin’, Journal of the American Chemical Society, 132(2), pp. 694–705. Available at: https://doi.org/10.1021/ja907974m.

Lewandowski, Józef R et al. (2010) ‘Measurement of site-specific 13C spin-lattice relaxation in a crystalline protein’, Journal of the American Chemical Society, 132(24), pp. 8252–4. Available at: https://doi.org/10.1021/ja102744b.

Nisius, L. (2010) Expression, purification and characterization of the HIV-1 coreceptor CCR5 and its ligand RANTES and high-pressure NMR investigation of hydrogen bonds in biomolecules. Available at: https://doi.org/10.5451/unibas-005398107.

Schönichen, André et al. (2010) ‘A flexible bipartite coiled coil structure is required for the interaction of Hexim1 with the P-TEFB subunit cyclin T1’, Biochemistry, 49(14), pp. 3083–91. Available at: https://doi.org/10.1021/bi902072f.

Vajpai, N. (2010) Structural characterization of the leukemia drug target ABL kinase and unfolded polypeptides by novel solution NMR techniques. Available at: https://doi.org/10.5451/unibas-005213609.

Vajpai, Navratna et al. (2010) ‘Side-chain chi(1) conformations in urea-denatured ubiquitin and protein G from (3)J coupling constants and residual dipolar couplings’, Journal of the American Chemical Society, 132(9), pp. 3196–203. Available at: https://doi.org/10.1021/ja910331t.

Zhang, Jianming et al. (2010) ‘Targeting Bcr-Abl by combining allosteric with ATP-binding-site inhibitors’, Nature, 463(7280), pp. 501–6. Available at: https://doi.org/10.1038/nature08675.

Grzesiek, S. and Sass, H. J. (2009) ‘From biomolecular structure to functional understanding : new NMR developments narrow the gap’, Current Opinion in Structural Biology, 19(5), pp. 585–595. Available at: https://doi.org/10.1016/j.sbi.2009.07.015.

Häussinger, Daniel, Huang, Jie-rong and Grzesiek, Stephan (2009) ‘DOTA-M8 : an extremely rigid, high-affinity lanthanide chelating tag for PCS NMR spectroscopy’, Journal of the American Chemical Society, 131(41), pp. 14761–7. Available at: https://doi.org/10.1021/ja903233w.

Jensen, M. R. et al. (2009) ‘Quantitative determination of the conformational properties of partially folded and intrinsically disordered proteins using NMR dipolar couplings’, Structure, 17(9), pp. 1169–85. Available at: https://doi.org/10.1016/j.str.2009.08.001.

Laage, S. et al. (2008) ‘Band-selective1H-13C cross-polarization in fast magic angle spinning solid-state NMR spectroscopy’, Journal of the American Chemical Society, 130(51), pp. 17216–17217. Available at: https://doi.org/10.1021/ja805926d.

Wang, Wei et al. (2008) ‘Structure and Dynamics of ¹³C,¹⁵N‐Labeled Lipopolysaccharides in a Membrane Mimetic’, Angewandte Chemie, 120(51), pp. 10018–10022. Available at: https://doi.org/10.1002/ange.200803474.

Dingley, Andrew J et al. (2008) ‘Direct detection of N−H⋯N hydrogen bonds in biomolecules by NMR spectroscopy’, Nature Protocols, 3(2), pp. 242–248. Available at: https://doi.org/10.1038/nprot.2007.497.

Adamczyk, Patrizia et al. (2008) ‘Minicollagen-15, a novel minicollagen isolated from Hydra, forms tubule structures in nematocysts’, Journal of molecular biology, 376(4), pp. 1008–20. Available at: https://doi.org/10.1016/j.jmb.2007.10.090.

Cordier, Florence et al. (2008) ‘Direct detection of N-H[...]O=C hydrogen bonds in biomolecules by NMR spectroscopy’, Nature Protocols, 3(2), pp. 235–41. Available at: https://doi.org/10.1038/nprot.2007.498.

Dames, Sonja A et al. (2008) ‘Insights into the low adhesive capacity of human T-cadherin from the NMR structure of Its N-terminal extracellular domain’, Journal of biological chemistry, 283(34), pp. 23485–95. Available at: https://doi.org/10.1074/jbc.m708335200.

Huang, Jie-Rong et al. (2008) ‘The extremely slow-exchanging core and acid-denatured state of green fluorescent protein’, HFSP Journal, 2(6), pp. 378–87. Available at: https://doi.org/10.2976/1.2976660.

Laage, Segolene et al. (2008) ‘Band-selective ¹H-¹³C cross-polarization in fast magic angle spinning solid-state NMR spectroscopy’, Journal of the American Chemical Society, 130(51), p. 17216–+. Available at: https://doi.org/10.1021/ja805926d.

Meier, Sebastian, Blackledge, Martin and Grzesiek, Stephan (2008) ‘Conformational distributions of unfolded polypeptides from novel NMR techniques’, Journal of Chemical Physics, 128(5), p. 052204. Available at: https://doi.org/10.1063/1.2838167.

Mrosek, Michael et al. (2008) ‘Structural analysis of B-Box 2 from MuRF1 : identification of a novel self-association pattern in a RING-like fold’, Biochemistry, 47(40), pp. 10722–30. Available at: https://doi.org/10.1021/bi800733z.

Nisius, Lydia et al. (2008) ‘Large-scale expression and purification of the major HIV-1 coreceptor CCR5 and characterization of its interaction with RANTES’, Protein expression and purification, 61(2), pp. 155–62. Available at: https://doi.org/10.1016/j.pep.2008.06.001.

Vajpai, Navratna et al. (2008) ‘Solution conformations and dynamics of ABL kinase-inhibitor complexes determined by NMR substantiate the different binding modes of imatinib/nilotinib and dasatinib’, Journal of biological chemistry, 283(26), pp. 18292–302. Available at: https://doi.org/10.1074/jbc.m801337200.

Vajpai, Navratna et al. (2008) ‘Backbone NMR resonance assignment of the Abelson kinase domain in complex with imatinib’, Biomolecular NMR Assignments, 2(1), pp. 41–2. Available at: https://doi.org/10.1007/s12104-008-9079-7.

Wang, W. et al. (2008) ‘Structure and dynamics of 13C,15N-labeled lipopolysaccharides in a membrane mimetic’, Angewandte Chemie. International edition in English, 47(51), pp. 9870–9874. Available at: https://doi.org/10.1002/anie.200803474.

Bang, Eunjung et al. (2007) ‘¹H, ¹³C, and ¹⁵N chemical shift assignments for the N-terminal extracellular domain of T-cadherin’, Journal of Biomolecular NMR, p. 179. Available at: https://doi.org/10.1007/s10858-006-9106-x.

Christen, Matthias et al. (2007) ‘DgrA is a member of a new family of cyclic diguanosine monophosphate receptors and controls flagellar motor function in Caulobacter crescentus’, Proceedings of the National Academy of Sciences of the United States of America, 104(10), pp. 4112–7. Available at: https://doi.org/10.1073/pnas.0607738104.

Dames, Sonja A et al. (2007) ‘Structure of the Cyclin T binding domain of Hexim1 and molecular basis for its recognition of P-TEFb’, Proceedings of the National Academy of Sciences of the United States of America, 104(36), pp. 14312–7. Available at: https://doi.org/10.1073/pnas.0701848104.

Duma, Luminita et al. (2007) ‘Recognition of RANTES by extracellular parts of the CCR5 receptor’, Journal of molecular biology, 365(4), pp. 1063–75. Available at: https://doi.org/10.1016/j.jmb.2006.10.040.

Huang, Jie-rong et al. (2007) ‘Stable intermediate states and high energy barriers in the unfolding of GFP’, Journal of molecular biology, 370(2), pp. 356–71. Available at: https://doi.org/10.1016/j.jmb.2007.04.039.

Meier, Sebastian, Grzesiek, Stephan and Blackledge, Martin (2007) ‘Mapping the conformational landscape of urea-denatured ubiquitin using residual dipolar couplings’, Journal of the American Chemical Society, 129(31), pp. 9799–807. Available at: https://doi.org/10.1021/ja0724339.

Meier, Sebastian et al. (2007) ‘Sequence-structure and structure-function analysis in cysteine-rich domains forming the ultrastable nematocyst wall’, Journal of molecular biology, 368(3), pp. 718–28. Available at: https://doi.org/10.1016/j.jmb.2007.02.026.

Meier, Sebastian et al. (2007) ‘Direct observation of dipolar couplings and hydrogen bonds across a beta-hairpin in 8 M urea’, Journal of the American Chemical Society, 129(4), pp. 754–5. Available at: https://doi.org/10.1021/ja067522k.

Meier, S. et al. (2007) ‘Continuous molecular evolution of protein-domain structures by single amino acid changes’, Current Biology, 17(2), pp. 173–8. Available at: https://doi.org/10.1016/j.cub.2006.10.063.

Sass, Hans-Jürgen, Schmid, Franziska Fang-Fang and Grzesiek, Stephan (2007) ‘Correlation of protein structure and dynamics to scalar couplings across hydrogen bonds’, Journal of the American Chemical Society, 129(18), pp. 5898–903. Available at: https://doi.org/10.1021/ja068336h.

Bax, Ad and Grzesiek , Stephan (2007) ‘Rotating frame Overhauser enhancement spectroscopy’, in Grant, David M.; Harris, R. K. (ed.) Encyclopedia of Nuclear Magnetic Resonance. New York: John Wiley (Encyclopedia of Nuclear Magnetic Resonance), pp. 245–257. Available at: https://doi.org/10.1002/9780470034590.emrstm0473.