[NMR paper] Proton Occupancies in Histidine Side Chains of Carbonic Anhydrase II by Neutron Crystallography and NMR - Differences, Similarities and Opportunities
Histidine is a key amino-acid residues in proteins that can exist in three different protonation states: two different neutral tautomeric forms and a protonated, positively charged one. It can act as both donor and acceptor of hydrogen bonds, coordinate metal ions, and engage in acid/base catalysis. Human Carbonic Anhydrase II (HCA II) is a pivotal enzyme catalyzing the reversible hydration of carbon dioxide. It contains 12 histidine residues: six surface exposed, two buried, three active site...
[NMR paper] Proton Transfer Kinetics in Histidine Side Chains Determined by pH-Dependent Multi-Nuclear NMR Relaxation
Proton Transfer Kinetics in Histidine Side Chains Determined by pH-Dependent Multi-Nuclear NMR Relaxation
Histidine is a key amino-acid residue in proteins with unique properties engendered by its imidazole side chain that can exist in three different states: two different neutral tautomeric forms and a protonated, positively charged one with a pK(a) value close to physiological pH. Commonly, two or all three states coexist and interchange rapidly, enabling histidine to act as both donor and acceptor of hydrogen bonds, coordinate metal ions, and engage in acid/base catalysis. Understanding...
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08-06-2024 09:57 AM
[NMR paper] XFEL structure of carbonic anhydrase II: a comparative study of XFEL, NMR, X-ray and neutron structures
XFEL structure of carbonic anhydrase II: a comparative study of XFEL, NMR, X-ray and neutron structures
The combination of X-ray free-electron lasers (XFELs) with serial femtosecond crystallography represents cutting-edge technology in structural biology, allowing the study of enzyme reactions and dynamics in real time through the generation of `molecular movies'. This technology combines short and precise high-energy X-ray exposure to a stream of protein microcrystals. Here, the XFEL structure of carbonic anhydrase II, a ubiquitous enzyme responsible for the interconversion of CO(2)...
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02-27-2024 09:30 PM
BEST and SOFAST experiments for resonance assignment of histidine and tyrosine side chains in 13 C/ 15 N labeled proteins
BEST and SOFAST experiments for resonance assignment of histidine and tyrosine side chains in 13 C/ 15 N labeled proteins
Abstract
Aromatic amino-acid side chains are essential components for the structure and function of proteins. We present herein a set of NMR experiments for time-efficient resonance assignment of histidine and tyrosine side chains in uniformly 13C/15N-labeled proteins. The use of band-selective 13C pulses allows to deal with linear chains of coupled spins, thus avoiding signal loss that occurs in branched spin systems during...
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11-25-2018 06:02 AM
Neutron Crystallography Detects Differences in ProteinDynamics: Structure of the PKG II Cyclic Nucleotide Binding Domainin Complex with an Activator
Neutron Crystallography Detects Differences in ProteinDynamics: Structure of the PKG II Cyclic Nucleotide Binding Domainin Complex with an Activator
https://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.8b00010/20180312/images/medium/bi-2018-00010h_0003.gif
Biochemistry
DOI: 10.1021/acs.biochem.8b00010
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http://feeds.feedburner.com/~r/acs/bichaw/~4/F7_wnrZBMNw
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03-13-2018 07:39 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
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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07-02-2011 05:30 AM
[NMR paper] Determination of pKa values of the histidine side chains of phosphatidylinositol-spec
Determination of pKa values of the histidine side chains of phosphatidylinositol-specific phospholipase C from Bacillus cereus by NMR spectroscopy and site-directed mutagenesis.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Determination of pKa values of the histidine side chains of phosphatidylinositol-specific phospholipase C from Bacillus cereus...
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08-22-2010 05:08 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...
Proton Occupancies in Histidine Side Chains of Carbonic Anhydrase II by Neutron Crystallography and NMR - Differences, Similarities and Opportunities
Linear Mode
