[NMR paper] The Mobility of Histidine Side Chains Analyzed with 15N NMR Relaxation and Cross-Correlation Data: Insight into Zinc-Finger - DNA Interactions.
Abstract
Due to chemical exchange, the mobility of histidine (His) side chains of proteins is typically difficult to analyze by NMR spectroscopy. Using an NMR approach that is uninfluenced by chemical exchange, we investigated internal motions of the His imidazole NH groups that directly interact with DNA phosphates in the Egr-1 zinc-finger - DNA complex. In this approach, the transverse and longitudinal cross-correlation rates for 15N chemical shift anisotropy (CSA) and 15N-1H dipole-dipole relaxation interference were analyzed together with 15N longitudinal relaxation rates and heteronuclear Overhauser effect data at two magnetic field strengths. We found that the zinc-coordinating His side chains directly interacting with DNA phosphates are strongly restricted in mobility. This makes a contrast to the arginine and lysine side chains that retain high mobility despite their interactions with DNA phosphates in the same complex. The entropic effects of side-chain mobility on molecular association are discussed.
PMID: 30963768 [PubMed - as supplied by publisher]
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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[NMR paper] NMR Scalar Couplings Across Intermolecular Hydrogen Bonds Between Zinc-Finger Histidine Side Chains and DNA Phosphate Groups.
NMR Scalar Couplings Across Intermolecular Hydrogen Bonds Between Zinc-Finger Histidine Side Chains and DNA Phosphate Groups.
NMR Scalar Couplings Across Intermolecular Hydrogen Bonds Between Zinc-Finger Histidine Side Chains and DNA Phosphate Groups.
J Phys Chem B. 2016 Sep 29;
Authors: Chattopadhyay A, Esadze A, Roy S, Iwahara J
Abstract
NMR scalar couplings across hydrogen bonds represent direct evidence of the partial covalent nature of hydrogen bonds and provide structural and dynamic information on hydrogen bonding. In...
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09-30-2016 10:11 AM
13C relaxation experiments for aromatic side chains employing longitudinal- and transverse-relaxation optimized NMR spectroscopy
13C relaxation experiments for aromatic side chains employing longitudinal- and transverse-relaxation optimized NMR spectroscopy
Abstract Aromatic side chains are prevalent in protein binding sites, perform functional roles in enzymatic catalysis, and form an integral part of the hydrophobic core of proteins. Thus, it is of great interest to probe the conformational dynamics of aromatic side chains and its response to biologically relevant events. Indeed, measurements of 13C relaxation rates in aromatic moieties have a long history in biomolecular NMR, primarily in the context of...
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07-05-2012 04:13 AM
Interactions of protein side chains with RNA defined with REDOR solid state NMR.
Interactions of protein side chains with RNA defined with REDOR solid state NMR.
Interactions of protein side chains with RNA defined with REDOR solid state NMR.
J Biomol NMR. 2011 Sep 25;
Authors: Huang W, Varani G, Drobny GP
Abstract
Formation of the complex between human immunodeficiency virus type-1 Tat protein and the transactivation response region (TAR) RNA is vital for transcriptional elongation, yet the structure of the Tat-TAR complex remains to be established. The NMR structures of free TAR, and TAR bound to Tat-derived...
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09-30-2011 05:59 AM
[NMR paper] Application of cross-correlated NMR spin relaxation to the zinc-finger protein CRP2(L
Application of cross-correlated NMR spin relaxation to the zinc-finger protein CRP2(LIM2): evidence for collective motions in LIM domains.
Related Articles Application of cross-correlated NMR spin relaxation to the zinc-finger protein CRP2(LIM2): evidence for collective motions in LIM domains.
Biochemistry. 2001 Aug 14;40(32):9596-604
Authors: Schüler W, Kloiber K, Matt T, Bister K, Konrat R
The solution structure of quail CRP2(LIM2) was significantly improved by using an increased number of NOE constraints obtained from a 13C,15N-labeled...
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11-19-2010 08:44 PM
[NMR paper] A study of protein side-chain dynamics from new 2H auto-correlation and 13C cross-cor
A study of protein side-chain dynamics from new 2H auto-correlation and 13C cross-correlation NMR experiments: application to the N-terminal SH3 domain from drk.
Related Articles A study of protein side-chain dynamics from new 2H auto-correlation and 13C cross-correlation NMR experiments: application to the N-terminal SH3 domain from drk.
J Mol Biol. 1998 Mar 13;276(5):939-54
Authors: Yang D, Mittermaier A, Mok YK, Kay LE
Two new NMR experiments are presented for measuring side-chain dynamics in proteins. The first method, requiring 15N, 13C,...
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11-17-2010 11:06 PM
[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] Zinc- and sequence-dependent binding to nucleic acids by the N-terminal zinc finger o
Zinc- and sequence-dependent binding to nucleic acids by the N-terminal zinc finger of the HIV-1 nucleocapsid protein: NMR structure of the complex with the Psi-site analog, dACGCC.
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 Zinc- and sequence-dependent binding to nucleic acids by the N-terminal zinc finger of the HIV-1 nucleocapsid protein: NMR...
The Mobility of Histidine Side Chains Analyzed with 15N NMR Relaxation and Cross-Correlation Data: Insight into Zinc-Finger - DNA Interactions.
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