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 the...
[NMR paper] Multi-Quantum Chemical Exchange Saturation Transfer NMR to Quantify Symmetrical Exchange: Application to Rotational Dynamics of the Guanidinium Group in Arginine Side Chains.
Multi-Quantum Chemical Exchange Saturation Transfer NMR to Quantify Symmetrical Exchange: Application to Rotational Dynamics of the Guanidinium Group in Arginine Side Chains.
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J Phys Chem Lett. 2020 Jun 16;:
Authors: Karunanithy G, Reinstein J, Hansen...
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[NMR paper] The Mobility of Histidine Side Chains Analyzed with 15N NMR Relaxation and Cross-Correlation Data: Insight into Zinc-Finger - DNA Interactions.
The Mobility of Histidine Side Chains Analyzed with 15N NMR Relaxation and Cross-Correlation Data: Insight into Zinc-Finger - DNA Interactions.
The Mobility of Histidine Side Chains Analyzed with 15N NMR Relaxation and Cross-Correlation Data: Insight into Zinc-Finger - DNA Interactions.
J Phys Chem B. 2019 Apr 09;:
Authors: Kemme CA, Luu RH, Chen C, Pletka CC, Pettitt BM, Iwahara J
Abstract
Due to chemical exchange, the mobility of histidine (His) side chains of proteins is typically difficult to analyze by NMR spectroscopy....
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04-10-2019 06:03 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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Site-SpecificProtonation Kinetics of Acidic SideChains in Proteins Determined by pH-Dependent Carboxyl 13C NMR Relaxation
Site-SpecificProtonation Kinetics of Acidic SideChains in Proteins Determined by pH-Dependent Carboxyl 13C NMR Relaxation
Johan Wallerstein, Ulrich Weininger, M. Ashhar I. Khan, Sara Linse and Mikael Akke
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja513205s/20150220/images/medium/ja-2014-13205s_0005.gif
Journal of the American Chemical Society
DOI: 10.1021/ja513205s
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[NMR paper] Site-specific protonation kinetics of acidic side chains in proteins determined by pH-dependent carboxyl 13C NMR relaxation.
Site-specific protonation kinetics of acidic side chains in proteins determined by pH-dependent carboxyl 13C NMR relaxation.
Related Articles Site-specific protonation kinetics of acidic side chains in proteins determined by pH-dependent carboxyl 13C NMR relaxation.
J Am Chem Soc. 2015 Feb 10;
Authors: Wallerstein J, Weininger U, Khan MA, Linse S, Akke M
Abstract
Proton transfer dynamics plays a critical role in many biochemical processes, such as proton pumping across membranes and enzyme catalysis. The large majority of enzymes...
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02-11-2015 04:19 PM
NMR Detection of pH-Dependent Histidine–Water Proton Exchange Reveals the Conduction Mechanism of a Transmembrane Proton Channel
NMR Detection of pH-Dependent Histidine–Water Proton Exchange Reveals the Conduction Mechanism of a Transmembrane Proton Channel
Fanghao Hu, Klaus Schmidt-Rohr and Mei Hong
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja2081185/aop/images/medium/ja-2011-081185_0008.gif
Journal of the American Chemical Society
DOI: 10.1021/ja2081185
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[NMR paper] Unfolding kinetics of tryptophan side chains in the dimerization and hinge regions of
Unfolding kinetics of tryptophan side chains in the dimerization and hinge regions of HIV-I protease tethered dimer by real time NMR spectroscopy.
Related Articles Unfolding kinetics of tryptophan side chains in the dimerization and hinge regions of HIV-I protease tethered dimer by real time NMR spectroscopy.
Biochem Biophys Res Commun. 2000 Mar 16;269(2):387-92
Authors: Panchal SC, Hosur RV
HIV I protease has been the target of extensive and variety of investigations in recent years because of its importance in the AIDS viral life cycle. We...
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[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...
Proton Transfer Kinetics in Histidine Side Chains Determined by pH-Dependent Multi-Nuclear NMR Relaxation
Linear Mode
