Fast Microsecond Dynamics of the Protein–Water Network in the Active Site of Human Carbonic Anhydrase II Studied by Solid-State NMR Spectroscopy - ACS Publications
Fast Microsecond Dynamics of the Protein–Water Network in the Active Site of Human Carbonic Anhydrase II Studied by Solid-State NMR Spectroscopy - ACS Publications
Fast Microsecond Dynamics of the Protein–Water Network in the Active Site of Human Carbonic Anhydrase II Studied by Solid-State NMR Spectroscopy - ACS Publications
[NMR paper] Unique epitope-antibody interactions in the intrinsically disordered proteoglycan-like domain of human carbonic anhydrase IX defined by high-resolution NMR combined with yeast surface display
Unique epitope-antibody interactions in the intrinsically disordered proteoglycan-like domain of human carbonic anhydrase IX defined by high-resolution NMR combined with yeast surface display
Carbonic anhydrase (CA)-IX is an extracellular enzyme that is essential in the adaptation of tumor cells to their increasingly more hypoxic and acidic microenvironment. Within the family of carbonic anhydrases, CA-IX is unique in that it is the only CA with an N-terminal intrinsically disordered region (IDR) containing a proteoglycan (PG)-like domain. This PG-like IDR has been described to be...
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[NMR paper] Microsecond dynamics in ubiquitin probed by solid-state NMR 15N R1rho relaxation experiments under fast MAS (60-110 kHz).
Microsecond dynamics in ubiquitin probed by solid-state NMR 15N R1rho relaxation experiments under fast MAS (60-110 kHz).
Related Articles Microsecond dynamics in ubiquitin probed by solid-state NMR 15N R1rho relaxation experiments under fast MAS (60-110 kHz).
Chemistry. 2017 Apr 20;:
Authors: Lakomek NA, Penzel S, Lends A, Cadalbert R, Ernst M, Meier BH
Abstract
15N R1? relaxation experiments in solid-state NMR are sensitive to timescales and amplitudes of internal protein motions in the hundreds of ns to µs time window,...
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04-21-2017 03:35 PM
[NMR paper] NMR Studies of Active-Site Properties of Human Carbonic Anhydrase II by using (15) N-Labeled 4-Methylimidazole as a Local Probe and Histidine Hydrogen-Bond Correlations.
NMR Studies of Active-Site Properties of Human Carbonic Anhydrase II by using (15) N-Labeled 4-Methylimidazole as a Local Probe and Histidine Hydrogen-Bond Correlations.
NMR Studies of Active-Site Properties of Human Carbonic Anhydrase II by using (15) N-Labeled 4-Methylimidazole as a Local Probe and Histidine Hydrogen-Bond Correlations.
Chemistry. 2014 Dec 17;
Authors: Shenderovich IG, Lesnichin SB, Tu C, Silverman DN, Tolstoy PM, Denisov GS, Limbach H
Abstract
By using a combination of liquid and solid-state NMR spectroscopy,...
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12-19-2014 11:42 AM
Site-Resolved Measurementof Microsecond-to-MillisecondConformational-Exchange Processes in Proteins by Solid-State NMR Spectroscopy
Site-Resolved Measurementof Microsecond-to-MillisecondConformational-Exchange Processes in Proteins by Solid-State NMR Spectroscopy
Martin Tollinger, Astrid C. Sivertsen, Beat H. Meier, Matthias Ernst and Paul Schanda
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja303591y/aop/images/medium/ja-2012-03591y_0005.gif
Journal of the American Chemical Society
DOI: 10.1021/ja303591y
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/ZVmFwVkbuRs
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08-29-2012 04:28 AM
Intrinsic Proton-Donating Power of Zinc-Bound Water in a Carbonic Anhydrase Active Site Model Estimated by NMR
Intrinsic Proton-Donating Power of Zinc-Bound Water in a Carbonic Anhydrase Active Site Model Estimated by NMR
Stepan B. Lesnichin, Ilya G. Shenderovich, Titin Muljati, David Silverman and Hans-Heinrich Limbach
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja203478j/aop/images/medium/ja-2011-03478j_0004.gif
Journal of the American Chemical Society
DOI: 10.1021/ja203478j
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/pgOKoZytT3U
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[NMR paper] Water-protein interactions in the molten-globule state of carbonic anhydrase b: an NM
Water-protein interactions in the molten-globule state of carbonic anhydrase b: an NMR spin-diffusion study.
Related Articles Water-protein interactions in the molten-globule state of carbonic anhydrase b: an NMR spin-diffusion study.
Protein Sci. 2000 Aug;9(8):1540-7
Authors: Kutyshenko VP, Cortijo M
We have used the homonuclear Overhauser effect (NOE) to characterize a model protein: carbonic anhydrase B. We have obtained NOE difference spectra for this protein, centering the on-resonance signals either at the methyl-proton or at the...
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11-19-2010 08:29 PM
[NMR paper] Sequential assignment of 1H, 13C and 15N resonances of human carbonic anhydrase I by
Sequential assignment of 1H, 13C and 15N resonances of human carbonic anhydrase I by triple-resonance NMR techniques and extensive amino acid-specific 15N-labeling.
Related Articles Sequential assignment of 1H, 13C and 15N resonances of human carbonic anhydrase I by triple-resonance NMR techniques and extensive amino acid-specific 15N-labeling.
J Biomol NMR. 1996 Dec;8(4):417-28
Authors: Sethson I, Edlund U, Holak TA, Ross A, Jonsson BH
The backbone NMR resonances of human carbonic anhydrase I (HCA I) have been assigned. This protein is one of...
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08-22-2010 02:20 PM
[NMR paper] Denatured states of human carbonic anhydrase II: an NMR study of hydrogen/deuterium e
Denatured states of human carbonic anhydrase II: an NMR study of hydrogen/deuterium exchange at tryptophan-indole-H(N) sites.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Denatured states of human carbonic anhydrase II: an NMR study of hydrogen/deuterium exchange at tryptophan-indole-H(N) sites.
FEBS Lett. 1999 Feb 26;445(2-3):361-5
Authors: Jonasson P, Kjellsson A, Sethson I, Jonsson BH
Hydrogen/deuterium (H/D) exchange measurements in low and moderate...
Fast Microsecond Dynamics of the Protein–Water Network in the Active Site of Human Carbonic Anhydrase II Studied by Solid-State NMR Spectroscopy - ACS Publications
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