Arginine side chains play critical roles in many proteinā??ligand interactions and enzyme catalysis. Unambiguous resonance assignment is a prerequisite for the nuclear magnetic resonance (NMR) spectroscopy studies of arginine side chains dynamics and hydrogen exchange properties from which one can expect to elucidate in more detail the roles of arginine residues in protein structure and function. Here we present a new mass spectrometry (MS)-based method for assigning the side-chain resonances of arginine residues in 2D 1Hā??15N NMR spectra. The method requires no additional isotopic labeling, and relies on knowledge of the amino acid sequence, the modification of the guanidino groups and liquid chromatographyā??mass spectrometry rather than the proteinā??s structure or properties. Correlating the modification rates can connect cross-peak positions from NMR data with MS data to support resonances assignments. In the present work, we have extended our original application to natural abundance human ubiquitin to provide Īµ-NH assessments of three arginine for this well-studied protein.
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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Impact of two-bond 15 Nā?? 15 N scalar couplings on 15 N transverse relaxation measurements for arginine side chains of proteins
Impact of two-bond 15 Nā?? 15 N scalar couplings on 15 N transverse relaxation measurements for arginine side chains of proteins
Abstract
NMR relaxation of arginine (Arg) 15NĪµ nuclei is useful for studying side-chain dynamics of proteins. In this work, we studied the impact of two geminal 15Nā??15N scalar couplings on measurements of transverse relaxation rates (R 2 ) for Arg side-chain 15NĪµ nuclei. For 12 Arg side chains of the DNA-binding domain of the Antp protein, we measured the geminal 15Nā??15N...
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05-29-2018 06:45 PM
[NMR paper] Determining rotational dynamics of the guanidino group of arginine side chains in proteins by carbon-detected NMR.
Determining rotational dynamics of the guanidino group of arginine side chains in proteins by carbon-detected NMR.
Related Articles Determining rotational dynamics of the guanidino group of arginine side chains in proteins by carbon-detected NMR.
Chem Commun (Camb). 2017 Aug 25;:
Authors: Gerecht K, Figueiredo AM, Hansen DF
Abstract
Arginine residues are imperative for many active sites and protein-interaction interfaces. A new NMR-based method is presented to determine the rotational dynamics around the N?-C? bond of...
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08-26-2017 03:38 PM
[NMR paper] Improved NMR experiments with (13)C-isotropic mixing for assignment of aromatic and aliphatic side chains in labeled proteins.
Improved NMR experiments with (13)C-isotropic mixing for assignment of aromatic and aliphatic side chains in labeled proteins.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles Improved NMR experiments with (13)C-isotropic mixing for assignment of aromatic and aliphatic side chains in labeled proteins.
J Biomol NMR. 2014 Jan 4;
Authors: Kovacs H, Gossert A
Abstract
Three improved (13)C-spinlock experiments for side chain assignments of...
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01-07-2014 11:16 PM
[NMR paper] Mass spectrometry assisted assignment of NMR resonances in 15N labeled proteins.
Mass spectrometry assisted assignment of NMR resonances in 15N labeled proteins.
Related Articles Mass spectrometry assisted assignment of NMR resonances in 15N labeled proteins.
J Am Chem Soc. 2004 Nov 10;126(44):14377-9
Authors: Feng L, Orlando R, Prestegard JH
Application of nuclear magnetic resonance (NMR) methods for the structural characterization to larger and more complex protein systems can be facilitated through the development of new methods for resonance assignment. Here, a novel approach that relies on integration of NMR and mass...
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11-24-2010 10:03 PM
[NMR paper] Extensive 1H NMR resonance assignment of proteins using natural abundance gradient-en
Extensive 1H NMR resonance assignment of proteins using natural abundance gradient-enhanced 13C-1H correlation spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Extensive 1H NMR resonance assignment of proteins using natural abundance gradient-enhanced 13C-1H correlation spectroscopy.
FEBS Lett. 1993 Nov 1;333(3):251-6
Authors: Medvedeva S, Simorre JP, Brutscher B, Guerlesquin F, Marion D
The reliability and completeness of 1H NMR resonance assignment can...
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08-22-2010 03:01 AM
[NMR paper] Assignment of the natural abundance 13C spectrum of proteins using 13C 1H-detected he
Assignment of the natural abundance 13C spectrum of proteins using 13C 1H-detected heteronuclear multiple-bond correlation NMR spectroscopy: structural information and stereospecific assignments from two- and three-bond carbon-hydrogen coupling constants.
Related Articles Assignment of the natural abundance 13C spectrum of proteins using 13C 1H-detected heteronuclear multiple-bond correlation NMR spectroscopy: structural information and stereospecific assignments from two- and three-bond carbon-hydrogen coupling constants.
Biochemistry. 1991 Oct 29;30(43):10457-66
...
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08-21-2010 11:12 PM
[NMR paper] Assignment of the natural abundance 13C spectrum of proteins using 13C 1H-detected he
Assignment of the natural abundance 13C spectrum of proteins using 13C 1H-detected heteronuclear multiple-bond correlation NMR spectroscopy: structural information and stereospecific assignments from two- and three-bond carbon-hydrogen coupling constants.
Related Articles Assignment of the natural abundance 13C spectrum of proteins using 13C 1H-detected heteronuclear multiple-bond correlation NMR spectroscopy: structural information and stereospecific assignments from two- and three-bond carbon-hydrogen coupling constants.
Biochemistry. 1991 Oct 29;30(43):10457-66
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Mass spectrometry assisted arginine side chains assignment of NMR resonances in natural abundance proteins
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