Related Articles15N NMR relaxation studies of calcium-loaded parvalbumin show tight dynamics compared to those of other EF-hand proteins.
Biochemistry. 1998 Jul 14;37(28):9964-75
Authors: Baldellon C, Alattia JR, Strub MP, Pauls T, Berchtold MW, Cavé A, Padilla A
Dynamics of the rat alpha-parvalbumin calcium-loaded form have been determined by measurement of 15N nuclear relaxation using proton-detected heteronuclear NMR spectroscopy. The relaxation data were analyzed using spectral density functions and the Lipari-Szabo formalism. The major dynamic features for the rat alpha-parvalbumin calcium-loaded form are (1) the extreme rigidity of the helix-loop-helix EF-hand motifs and the linker segment connecting them, (2) the N and C termini of the protein being restricted in their mobility, (3) a conformational exchange occurring at the kink of helix D, and (4) the residue at relative position 2 in the Ca2+-binding sites having an enhanced mobility. Comparison of the Ca2+-binding EF-hand domains of alpha-parvalbumin-Ca2+, calbindin-Ca2+, and calmodulin-Ca2+ shows that parvalbumin is probably the most rigid of the EF-hand proteins. It also illustrates the dynamical properties which are conserved in the EF-hand domains from different members of this superfamily: (1) a tendency toward higher mobility of NH vectors at relative position 2 in the Ca2+-binding loop, (2) a restricted mobility for the other residues in the binding loop, and (3) an overall rigidity for the helices of EF-hand motifs. The differences in mobility between parvalbumin and the two EF-hand proteins occur mainly at the linker connecting the pair of EF hands and also at the C terminus of the last helix. In parvalbumin-Ca2+, these two regions are characterized by a pronounced rigidity compared to the corresponding more mobile regions in calbindin-Ca2+ and calmodulin-Ca2+.
Recent Developments in (15)N NMR Relaxation Studies that Probe Protein Backbone Dynamics.
Recent Developments in (15)N NMR Relaxation Studies that Probe Protein Backbone Dynamics.
Recent Developments in (15)N NMR Relaxation Studies that Probe Protein Backbone Dynamics.
Top Curr Chem. 2011 Sep 7;
Authors: Ishima R
Abstract
Nuclear Magnetic Resonance (NMR) relaxation is a powerful technique that provides information about internal dynamics associated with configurational energetics in proteins, as well as site-specific information involved in conformational equilibria. In particular, (15)N relaxation is a useful probe to...
nmrlearner
Journal club
0
09-08-2011 06:50 PM
[NMR paper] Mutational, NMR, and NH exchange studies of the tight and selective binding of 8-oxo-
Mutational, NMR, and NH exchange studies of the tight and selective binding of 8-oxo-dGMP by the MutT pyrophosphohydrolase.
Related Articles Mutational, NMR, and NH exchange studies of the tight and selective binding of 8-oxo-dGMP by the MutT pyrophosphohydrolase.
Biochemistry. 2004 Mar 30;43(12):3404-14
Authors: Saraswat V, Azurmendi HF, Mildvan AS
The solution structure of the ternary MutT enzyme-Mg(2+)-8-oxo-dGMP complex showed the proximity of Asn119 and Arg78 and the modified purine ring of 8-oxo-dGMP, suggesting specific roles for...
nmrlearner
Journal club
0
11-24-2010 09:25 PM
[NMR paper] Backbone dynamics of the c-Jun leucine zipper: 15N NMR relaxation studies.
Backbone dynamics of the c-Jun leucine zipper: 15N NMR relaxation studies.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Backbone dynamics of the c-Jun leucine zipper: 15N NMR relaxation studies.
Biochemistry. 1996 Apr 16;35(15):4867-77
Authors: MacKay JP, Shaw GL, King GF
The backbone dynamics of the coiled-coil leucine zipper domain of c-Jun have been studied using proton-detected two-dimensional 1H-15N NMR spectroscopy. Longitudinal (T1) and transverse (T2) 15N relaxation times,...
nmrlearner
Journal club
0
08-22-2010 02:27 PM
[NMR paper] Rotational dynamics of calcium-free calmodulin studied by 15N-NMR relaxation measurem
Rotational dynamics of calcium-free calmodulin studied by 15N-NMR relaxation measurements.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles Rotational dynamics of calcium-free calmodulin studied by 15N-NMR relaxation measurements.
Eur J Biochem. 1995 Jun 15;230(3):1014-24
Authors: Tjandra N, Kuboniwa H, Ren H, Bax A
The backbone motions of calcium-free Xenopus calmodulin have been characterized by measurements of the 15N...
nmrlearner
Journal club
0
08-22-2010 03:41 AM
[NMR paper] NMR structural studies of the tight complex between a trifluoromethyl ketone inhibito
NMR structural studies of the tight complex between a trifluoromethyl ketone inhibitor and the 85-kDa human phospholipase A2.
Related Articles NMR structural studies of the tight complex between a trifluoromethyl ketone inhibitor and the 85-kDa human phospholipase A2.
Biochemistry. 1993 Nov 30;32(47):12560-5
Authors: Trimble LA, Street IP, Perrier H, Tremblay NM, Weech PK, Bernstein MA
Arachidonyl trifluoromethyl ketone (AACOCF3) is a slow- and tight-binding inhibitor of the human cytosolic phospholipase A2 (cPLA2) . 19F and 13C NMR...
nmrlearner
Journal club
0
08-22-2010 03:01 AM
[NMR paper] 15N NMR relaxation studies of the FK506 binding protein: backbone dynamics of the unc
15N NMR relaxation studies of the FK506 binding protein: backbone dynamics of the uncomplexed receptor.
Related Articles 15N NMR relaxation studies of the FK506 binding protein: backbone dynamics of the uncomplexed receptor.
Biochemistry. 1993 Sep 7;32(35):9000-10
Authors: Cheng JW, Lepre CA, Chambers SP, Fulghum JR, Thomson JA, Moore JM
Backbone dynamics of the major tacrolimus (FK506) binding protein (FKBP-12, 107 amino acids) have been studied using 15N relaxation data derived from proton-detected two-dimensional 1H-15N NMR spectroscopy....
nmrlearner
Journal club
0
08-22-2010 03:01 AM
[NMR paper] Backbone dynamics of calcium-loaded calbindin D9k studied by two-dimensional proton-d
Backbone dynamics of calcium-loaded calbindin D9k studied by two-dimensional proton-detected 15N NMR spectroscopy.
Related Articles Backbone dynamics of calcium-loaded calbindin D9k studied by two-dimensional proton-detected 15N NMR spectroscopy.
Biochemistry. 1992 May 26;31(20):4856-66
Authors: Kördel J, Skelton NJ, Akke M, Palmer AG, Chazin WJ
Backbone dynamics of calcium-loaded calbindin D9k have been investigated by two-dimensional proton-detected heteronuclear nuclear magnetic resonance spectroscopy, using a uniformly 15N enriched...
nmrlearner
Journal club
0
08-21-2010 11:41 PM
[NMR paper] Synthesis of 5-methylaminomethyl-2-selenouridine in tRNAs: 31P NMR studies show the l
Synthesis of 5-methylaminomethyl-2-selenouridine in tRNAs: 31P NMR studies show the labile selenium donor synthesized by the selD gene product contains selenium bonded to phosphorus.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Synthesis of 5-methylaminomethyl-2-selenouridine in tRNAs: 31P NMR studies show the labile selenium donor synthesized by the selD gene product contains selenium bonded to phosphorus.
Proc Natl Acad Sci U S A. 1992 Apr 1;89(7):2975-9
Authors: ...
15N NMR relaxation studies of calcium-loaded parvalbumin show tight dynamics compared
Linear Mode
