Altieri AS, Hinton DP, Byrd RA (1995) Association of biomolecular systems via pulsed-field gradient NMR self-diffusion measurements. J Am Chem Soc 117:7566–7567. https://doi.org/10.1021/ja00133a039

Article  ADS  Google Scholar 

Augé S, Schmit P-O, Crutchfield CA, Islam MT, Harris DJ, Durand E, Clemancey M, Quoineaud A-A, Lancelin J-M, Prigent Y, Taulelle F, Delsuc M-A (2009) NMR measure of translational diffusion and fractal dimension. Application to molecular mass measurement. J Phys Chem B 113:1914–1918. https://doi.org/10.1021/jp8094424

Article  Google Scholar 

Augustyniak R, Ferrage F, Paquin R, Lequin O, Bodenhausen G (2011) Methods to determine slow diffusion coefficients of biomolecules. Applications to Engrailed 2, a partially disordered protein. J Biomol NMR 50:209–218. https://doi.org/10.1007/s10858-011-9510-8

Article  Google Scholar 

Augustyniak R, Ferrage F, Damblon C, Bodenhausen G, Pelupessy P (2012) Efficient determination of diffusion coefficients by monitoring transport during recovery delays in NMR. Chem Commun 48:5307–5309. https://doi.org/10.1039/c2cc30578j

Article  Google Scholar 

Balbach J (2000) Compaction during protein folding studied by real-time NMR diffusion experiments. J Am Chem Soc 122:5887–5888. https://doi.org/10.1021/ja994514d

Article  ADS  Google Scholar 

Baldwin AJ, Hilton GR, Lioe H, Bagneris C, Benesch JLP, Kay LE (2011) Quaternary dynamics of alpha B-crystallin as a direct consequence of localised tertiary fluctuations in the C-terminus. J Mol Biol 413:310–320. https://doi.org/10.1016/j.jmb.2011.07.017

Article  Google Scholar 

Barhoum S, Yethiraj A (2010) NMR detection of an equilibrium phase consisting of monomers and clusters in concentrated lysozyme solutions. J Phys Chem B 114:17062–17067. https://doi.org/10.1021/jp108995k

Article  Google Scholar 

Brady JP, Farber PJ, Sekhar A, Lin Y-H, Huang R, Bah A, Nott TJ, Chan HS, Baldwin AJ, Forman-Kay JD, Kay LE (2017) Structural and hydrodynamic properties of an intrinsically disordered region of a germ cell-specific protein on phase separation. Proc Natl Acad Sci U S A 114:E8194–E8203. https://doi.org/10.1073/pnas.1706197114

Article  Google Scholar 

Bruker (2020) TopSpin. User Manual. Version 012. Bruker Corporation, Billerica MA, USA

Google Scholar 

Buevich AV, Baum J (2002) Residue-specific real-time NMR diffusion experiments define the association states of proteins during folding. J Am Chem Soc 124:7156–7162. https://doi.org/10.1021/ja012699u

Article  ADS  Google Scholar 

Chan SHS, Waudby CA, Cassaignau AME, Cabrita LD, Christodoulou J (2015) Increasing the sensitivity of NMR diffusion measurements by paramagnetic longitudinal relaxation enhancement, with application to ribosome-nascent chain complexes. J Biomol NMR 63:151–163. https://doi.org/10.1007/s10858-015-9968-x

Article  Google Scholar 

Chevelkov V, Xue Y, Rao DK, Forman-Kay JD, Skrynnikov NR (2010) 15NH/D-SOLEXSY experiment for accurate measurement of amide solvent exchange rates. Application to denatured drkN SH3. J Biomol NMR 46(3):227–244. https://doi.org/10.1007/s10858-010-9398-8

Article  Google Scholar 

Choy WY, Mulder FAA, Crowhurst KA, Muhandiram DR, Millett IS, Doniach S, Forman-Kay JD, Kay LE (2002) Distribution of molecular size within an unfolded state ensemble using small-angle X-ray scattering and pulse field gradient NMR techniques. J Mol Biol 316:101–112. https://doi.org/10.1006/jmbi.2001.5328

Article  Google Scholar 

Christodoulou J, Larsson G, Fucini P, Connell SR, Pertinhez TA, Hanson CL, Redfield C, Nierhaus KH, Robinson CV, Schleucher J, Dobson CM (2004) Heteronuclear NMR investigations of dynamic regions of intact Escherichia coli ribosomes. Proc Natl Acad Sci U S A 101:10949–10954. https://doi.org/10.1073/pnas.0400928101

Article  ADS  Google Scholar 

Cobas C (2018) Applications of the Whittaker smoother in NMR spectroscopy. Magn Reson Chem 56:1140–1148. https://doi.org/10.1002/mrc.4747

Article  Google Scholar 

Cobas CJ, Bernstein MA, Martín-Pastor M, Tahoces PG (2006) A new general-purpose fully automatic baseline-correction procedure for 1D and 2D NMR data. J Magn Reson 183:145–151. https://doi.org/10.1016/j.jmr.2006.07.013

Article  ADS  Google Scholar 

Coffman JL, Lightfoot EN, Root TW (1997) Protein diffusion in porous chromatographic media studied by proton and fluorine PFG-NMR. J Phys Chem B 101:2218–2223. https://doi.org/10.1021/jp962585i

Article  Google Scholar 

Dalvit C, Vulpetti A (2012) Technical and practical aspects of 19F NMR-based screening: toward sensitive high-throughput screening with rapid deconvolution. Magn Reson Chem 50:592–597. https://doi.org/10.1002/mrc.3842

Article  Google Scholar 

Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A (1995) NMRPipe: a multidimensional spectral processing system based on Unix pipes. J Biomol NMR 6:277–293. https://doi.org/10.1007/BF00197809

Article  Google Scholar 

Demers JP, Mittermaier A (2009) Binding mechanism of an SH3 domain studied by NMR and ITC. J Am Chem Soc 131:4355–4367. https://doi.org/10.1021/ja808255d

Article  ADS  Google Scholar 

Didenko T, Boelens R, Rudiger SGD (2011) 3D DOSY-TROSY to determine the translational diffusion coefficient of large protein complexes. Protein Eng Des Sel 24:99–103. https://doi.org/10.1093/protein/gzq091

Article  Google Scholar 

Dobson CM, Evans PA, Williamson KL (1984) Proton NMR studies of denatured lysozyme. FEBS Lett 168:331–334. https://doi.org/10.1016/0014-5793(84)80273-2

Article  Google Scholar 

Edwards LJ, Savostyanov DV, Welderufael ZT, Lee D, Kuprov I (2014) Quantum mechanical NMR simulation algorithm for protein-size spin systems. J Magn Reson 243:107–113. https://doi.org/10.1016/j.jmr.2014.04.002

Article  ADS  Google Scholar 

Ernst RR, Bodenhausen G, Wokaun A (1987) Principles of nuclear magnetic resonance in one and two dimensions. Oxford University Press, Oxford

Google Scholar 

Ferrage F, Zoonens M, Warschawski DE, Popot J-L, Bodenhausen G (2003) Slow diffusion of macromolecular assemblies by a new pulsed field gradient NMR method. J Am Chem Soc 125:2541–2545. https://doi.org/10.1021/ja0211407

Article  ADS  Google Scholar 

Grage H, Akke M (2003) A statistical analysis of NMR spectrometer noise. J Magn Reson 162:176–188. http://dx.doi.org/https://https://doi.org/10.1016/S1090-7807(03)00038-7

Article  ADS  Google Scholar 

Hansen DF, Yang D, Feng H, Zhou Z, Wiesner S, Bai Y, Kay LE (2007) An exchange-free measure of 15N transverse relaxation: an NMR spectroscopy application to the study of a folding intermediate with pervasive chemical exchange. J Am Chem Soc 129:11468–11479. https://doi.org/10.1021/ja072717t

Article  ADS  Google Scholar 

Helmus JJ, Jaroniec CP (2013) Nmrglue: an open source python package for the analysis of multidimensional NMR data. J Biomol NMR 55:355–367. https://doi.org/10.1007/s10858-013-9718-x

Article  Google Scholar 

Hoffmann ARF, Caillon L, Salazar Vazquez LS, Spath PA, Carlier L, Khemtémourian L, Lequin O (2018) Time dependence of NMR observables reveals salient differences in the accumulation of early aggregated species between human islet amyloid polypeptide and amyloid-β. Phys Chem Chem Phys 20:9561–9573. https://doi.org/10.1039/c7cp07516b

Article  Google Scholar 

Horst R, Horwich AL, Wüthrich K (2011) Translational diffusion of macromolecular assemblies measured using transverse-relaxation-optimized pulsed field gradient NMR. J Am Chem Soc 133:16354–16357. https://doi.org/10.1021/ja206531c

Article  ADS  Google Scholar 

Huang R, Ripstein ZA, Augustyniak R, Lazniewski M, Ginalski K, Kay LE, Rubinstein JL (2016) Unfolding the mechanism of the AAA plus unfoldase VAT by a combined cryo-EM, solution NMR study. Proc Natl Acad Sci U S A 113:E4190–E4199. https://doi.org/10.1073/pnas.1603980113

Article  ADS  Google Scholar 

Huang R, Brady JP, Sekhar A, Yuwen T, Kay LE (2017) An enhanced sensitivity methyl 1H triple-quantum pulse scheme for measuring diffusion constants of macromolecules. J Biomol NMR 68:249–255. https://doi.org/10.1007/s10858-017-0122-9

Article  Google Scholar 

Ilyina E, Roongta V, Pan H, Woodward C, Mayo KH (1997) A pulsed-field gradient NMR study of bovine pancreatic trypsin inhibitor self-association. Biochemistry 36:3383–3388. https://doi.org/10.1021/bi9622229

Article  Google Scholar 

Jerschow A, Muller N (1997) Suppression of convection artifacts in stimulated-echo diffusion experiments. Double-stimulated-echo experiments. J Magn Reson 125:372–375. https://doi.org/10.1006/jmre.1997.1123

Article  ADS  Google Scholar 

Kato H, Gruschus J, Ghirlando R, Tjandra N, Bai Y (2009) Characterization of the N-terminal tail domain of histone H3 in condensed nucleosome arrays by hydrogen exchange and NMR. J Am Chem Soc 131:15104–15105. https://doi.org/10.1021/ja9070078

Article  ADS  Google Scholar 

Kharkov BB, Podkorytov IS, Bondarev SA, Belousov MV, Salikov VA, Zhouravleva GA, Skrynnikov NR (2021) The role of rotational motion in diffusion NMR experiments on supramolecular assemblies: application to Sup35NM fibrils. Angew. Chem Int Ed 60:15445–15451. https://doi.org/10.1002/anie.202102408

Article  Google Scholar 

Kheddo P, Cliff MJ, Uddin S, van der Walle CF, Golovanov AP (2016) Characterizing monoclonal antibody formulations in arginine glutamate solutions using 1H NMR spectroscopy. Mabs 8:1245–1258.