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Nietlispach Group

NMR spectroscopy of membrane proteins

Studying at Cambridge

 

Publications

 Selected Publications

Time-domain signal modelling in multidimensional NMR experiments for estimation of relaxation parameters
Yevgen Matviychuk, Mark J. Bostock, Daniel Nietlispach, Daniel J. Holland, Journal of Biomolecular NMR (2019) 73, 93-104
(doi: 10.1007/s10858-018-00224-2)

Characterisation of denatured states of sensory rhodopsin II by solution-state NMR
Yi Lei Tan, James Mitchell, Judith Klein-Seetharaman, Daniel Nietlispach, Journal of Molecular Biology (2019) 431, 2790-2809
(doi: 10.1016/j.jmb.2019.04.039)

Compressed sensing: Reconstruction of non‐uniformly sampled multidimensional NMR data
Mark Bostock and Daniel Nietlispach, Concepts in Magnetic Resonance: Part A (2018) 46A, e21438 (from special issue: Topics in NMR Data Processing)
(doi: 10.1002/cmr.a.21438)

Characterisation of denatured states and reversible unfolding of sensory rhodopsin II
Yi Lei Tan, James Mitchell, Judith Klein-Seetharaman, Daniel Nietlispach, Journal of Molecular Biology (2018) 430, 4068-4086
(doi: 10.1016/j.jmb.2018.07.031)

A generalized approach for NMR studies of lipid-protein interactions based on sparse fluorination of acyl chains.
Alfredo De Biasio, Alain Ibáñez de Opakua, Mark J. Bostock, Daniel Nietlispach, Tammo Diercks and Francisco J. Blanco, Chemical Communications (2018) 54, 7306-7309
(doi: 10.1039/C8CC02483A)

Insight into partial agonism by observing multiple equilibria for ligand-bound and Gs-mimetic nanobody-bound β1-adrenergic receptor.
Andras S. Solt, Mark J. Bostock, Binesh Shrestha, Prashant Kumar, Tony Warne, Christopher G. Tate, and Daniel Nietlispach, Nature Communications (2017) 28, 1795
(doi: 10.1038/s41467-017-02008-y)

An adaptable phospholipid membrane mimetic system for solution NMR studies of membrane proteins.
Chih-Ta Henry Chien, Lukas R. Helfinger, Mark J. Bostock, Andras Solt, Yi Lei Tan, and Daniel Nietlispach, Journal of the American Chemical Society (2017) 139, 14829-14832
(doi: 10.1021/jacs.7b06730)

Compressed Sensing ℓ1-Norm Minimisation in Multidimensional NMR Spectroscopy.
Mark J. Bostock, Daniel J. Holland and Daniel Nietlispach, from Fast NMR Data Acquisition - Beyond the Fourier Transform (RSC publishing) (2017)
(doi:10.1039/9781782628361-00267)

Improving resolution in multidimensional NMR using random quadrature detection with compressed sensing reconstruction.
Mark J. Bostock, Daniel J. Holland, Daniel Nietlispach, Journal of Biomolecular NMR (2017) 68, 67-77
(doi:10.1007/s10858-016-0062-9)

Application of random coherence order selection in gradient-enhanced multidimensional NMR.
Mark J. Bostock and Daniel Nietlispach, Journal of Physics Conference Series (2016) 699:012004
(doi:10.1088/1742-6596/699/1/012004)

Integral membrane protein structure determination using pseudocontact shifts.
Duncan J. Crick, Jue X. Wang, Bim Graham, James D. Swarbrick, Helen R. Mott, Daniel Nietlispach, Journal of Biomolecular NMR (2015) 61, 197-207
(doi:10.1007/s10858-015-9899-6)

Detergent-free mass spectrometry of membrane protein complexes.
Jonathan T. S. Hopper, Yvonne Ting-Chun Yu, Dianfan Li, Alison Raymond, Mark Bostock, Idlir Liko, Victor Mikhailov, Arthur Laganowsky, Justin L P Benesch, Martin Caffrey, Daniel Nietlispach, Carol V. Robinson, Nature Methods (2013), 10, 1206-1208
(doi:10.1038/nmeth.2691)

Compressed sensing reconstruction of undersampled 3D NOESY spectra: application to large membrane proteins.
Mark J. Bostock, Daniel J. Holland, Daniel Nietlispach, Journal of Biomolecular NMR (2012), 54, 15-32
(doi:10.1007/s10858-012-9643-4)

NMR of membrane proteins.
Mark Bostock and Daniel Nietlispach, from Recent Developments in Biomoecular NMR (RSC publishing) (2012)
(doi:10.1039/9781849735391-00271)

Solution NMR studies of integral polytopic α-helical membrane proteins: The structure determination of the seven-helix transmembrane receptor sensory rhodopsin II, pSRII.
Antoine Gautier and Daniel Nietlispach, Methods in Molecular Biology (2012), 914, 25-45
(doi:10.1007/978-1-62703-23-6_3)
Fast multidimensional NMR spectroscopy using compressed sensing.
Daniel J. Holland, Mark J. Bostock, Lynn F. Gladden, Daniel Nietlispach, Angewandte Chemie International Edition (2011), 50,6548-6551
(doi:10.1002/anie.201100440)
Solution NMR studies of polytopic α-helical membrane proteins.
Daniel Nietlispach and Antoine Gautier, Current Opinion in Structural Biology (2011), 21, 497-508
(doi:10.1016/j.sbi.2011.06.009)

NMR analysis of the structure, dynamics, and unique oligomerization properties of the chemokine CCL27.
Ariane L. Jansma, John P. Kirkpatrick, Andro R. Hsu, Tracy M. Handel, and Daniel Nietlispach, Journal of Biological Chemistry (2010), 285, 14424-14437.
(doi:10.1074/jbc.M109.091108)

Structure determination of the seven-helix transmembrane receptor sensory rhodopsin II by solution NMR spectroscopy.
Antoine Gautier, Helen R. Mott, Mark J. Bostock, John P. Kirkpatrick, Daniel Nietlispach, Nature Structural and Molecular Biology (2010), 17, 768-774
(doi:10.1038/nsmb.1807)
Solution-state NMR spectroscopy of a seven-helix transmembrane protein receptor: backbone assignment, secondary structure, and dynamics.
Antoine Gautier, John P. Kirkpatrick, Daniel Nietlispach, Angewandte Chemie International Edition (2008), 47, 7297-7300
(doi:10.1002/anie.200802783)
Suppression of anti-TROSY lines in a sensitivity enhanced gradient selection.
Daniel Nietlispach, Journal of Biomolecular NMR (2005), 31, 161-166
(doi:10.1007/s10858-004-8195-7)
A selective intra-HN(CA)CO experiment for the backbone assignment of deuterated proteins.
Daniel Nietlispach, Journal of Biomolecular NMR (2004), 28,131-136
(doi:10.1023/B:JNMR.0000013829.17620.39)
Ultra-high resolution 3D NMR spectra from limited-size data sets.
Jianhan Chen, Daniel Nietlispach, A.J Shaka, Vladimir A. Mandelshtam, Journal of Magnetic Resonance (2004), 169, 215-224.
(doi:10.1016/j.jmr.2004.04.017)
A novel approach for the sequential backbone assignment of larger proteins: Selective intra-HNCA and DQ-HNCA.
Daniel Nietlispach, Yutaka Ito and Ernest D. Laue, Journal of the American Chemical Society (2002), 124, 11199-11207.
(doi:10.1021/ja025865m)