Related ArticlesBackbone dynamics of the calcium-signaling protein apo-S100B as determined by 15N NMR relaxation.
Biochemistry. 2001 Mar 27;40(12):3439-48
Authors: Inman KG, Baldisseri DM, Miller KE, Weber DJ
Backbone dynamics of homodimeric apo-S100B were studied by (15)N nuclear magnetic resonance relaxation at 9.4 and 14.1 T. Longitudinal relaxation (T(1)), transverse relaxation (T(2)), and the (15)N-[(1)H] NOE were measured for 80 of 91 backbone amide groups. Internal motional parameters were determined from the relaxation data using the model-free formalism while accounting for diffusion anisotropy. Rotational diffusion of the symmetric homodimer has moderate but statistically significant prolate axial anisotropy (D( parallel)/D( perpendicular) = 1.15 +/- 0.02), a global correlation time of tau(m) = 7.80 +/- 0.03 ns, and a unique axis in the plane normal to the molecular symmetry axis. Of 29 residues at the dimer interface (helices 1 and 4), only one has measurable internal motion (Q71), and the order parameters of the remaining 28 were the highest in the protein (S(2) = 0.80 to 0.91). Order parameters in the typical EF hand calcium-binding loop (S(2) = 0.73 to 0.87) were slightly lower than in the pseudo-EF hand (S(2) = 0.75 to 0.89), and effective internal correlation times, tau(e), distinct from global tumbling, were detected in the calcium-binding loops. Helix 3, which undergoes a large, calcium-induced conformational change necessary for target-protein binding, does not show evidence of interchanging between the apo and Ca(2+)-bound orientations in the absence of calcium but has rapid motion in several residues throughout the helix (S(2) = 0.78 to 0.88; 10 < or = tau(e) < or = 30 ps). The lowest order parameters were found in the C-terminal tail (S(2) = 0.62 to 0.83). Large values for chemical exchange also occur in this loop and in regions nearby in space to the highly mobile C-terminal loop, consistent with exchange broadening effects observed.
Local protein backbone folds determined by calculated NMR chemical shifts.
Local protein backbone folds determined by calculated NMR chemical shifts.
Local protein backbone folds determined by calculated NMR chemical shifts.
J Comput Chem. 2011 Sep 9;
Authors: Czajlik A, Hudáky I, Perczel A
Abstract
NMR chemical shifts (CSs: ?N(NH) , ?C(?) , ?C(?) , ?C', ?H(NH) , and ?H(?) ) were computed for the amino acid backbone conformers (?(L) , ?(L) , ?(L) , ?(L) , ?(L) , ?(D) , ?(D) , ?(D) , and ?(D) ) modeled by oligoalanine structures. Topological differences of the extended fold were investigated on single ?-strands,...
nmrlearner
Journal club
0
09-10-2011 06:51 PM
[NMR paper] Location of the Zn(2+)-binding site on S100B as determined by NMR spectroscopy and si
Location of the Zn(2+)-binding site on S100B as determined by NMR spectroscopy and site-directed mutagenesis.
Related Articles Location of the Zn(2+)-binding site on S100B as determined by NMR spectroscopy and site-directed mutagenesis.
Biochemistry. 2003 Nov 25;42(46):13410-21
Authors: Wilder PT, Baldisseri DM, Udan R, Vallely KM, Weber DJ
In addition to binding Ca(2+), the S100 protein S100B binds Zn(2+) with relatively high affinity as confirmed using isothermal titration calorimetry (ITC; K(d) = 94 +/- 17 nM). The Zn(2+)-binding site on...
nmrlearner
Journal club
0
11-24-2010 09:16 PM
[NMR paper] Shape and dynamics of a calcium-binding protein investigated by nitrogen-15 NMR relax
Shape and dynamics of a calcium-binding protein investigated by nitrogen-15 NMR relaxation.
Related Articles Shape and dynamics of a calcium-binding protein investigated by nitrogen-15 NMR relaxation.
Methods Mol Biol. 2002;173:285-300
Authors: Werner JM, Campbell ID, Downing AK
nmrlearner
Journal club
0
11-24-2010 08:49 PM
[NMR paper] Three-dimensional solution structure of the calcium-signaling protein apo-S100A1 as d
Three-dimensional solution structure of the calcium-signaling protein apo-S100A1 as determined by NMR.
Related Articles Three-dimensional solution structure of the calcium-signaling protein apo-S100A1 as determined by NMR.
Biochemistry. 2002 Jan 22;41(3):788-96
Authors: Rustandi RR, Baldisseri DM, Inman KG, Nizner P, Hamilton SM, Landar A, Landar A, Zimmer DB, Weber DJ
S100A1, a member of the S100 protein family, is an EF-hand containing Ca(2+)-binding protein (93 residues per subunit) with noncovalent interactions at its dimer interface. Each...
nmrlearner
Journal club
0
11-24-2010 08:49 PM
[NMR paper] Backbone dynamics of the 269-residue protease Savinase determined from 15N-NMR relaxa
Backbone dynamics of the 269-residue protease Savinase determined from 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 Backbone dynamics of the 269-residue protease Savinase determined from 15N-NMR relaxation measurements.
Eur J Biochem. 1996 Feb 1;235(3):629-40
Authors: Remerowski ML, Pepermans HA, Hilbers CW, Van De Ven FJ
Backbone dynamics of Savinase, a subtilisin of 269 residues secreted by...
nmrlearner
Journal club
0
08-22-2010 02:27 PM
[NMR paper] Solution structure of rat apo-S100B(beta beta) as determined by NMR spectroscopy.
Solution structure of rat apo-S100B(beta beta) as determined by NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Solution structure of rat apo-S100B(beta beta) as determined by NMR spectroscopy.
Biochemistry. 1996 Sep 10;35(36):11577-88
Authors: Drohat AC, Amburgey JC, Abildgaard F, Starich MR, Baldisseri D, Weber DJ
S100B(beta beta), a member of the S100 protein family, is a Ca(2+)-binding protein with noncovalent interactions at its dimer interface. Each apo-S100 beta...
nmrlearner
Journal club
0
08-22-2010 02:20 PM
[NMR paper] Solution secondary structure of calcium-saturated troponin C monomer determined by mu
Solution secondary structure of calcium-saturated troponin C monomer determined by multidimensional heteronuclear NMR spectroscopy.
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 Solution secondary structure of calcium-saturated troponin C monomer determined by multidimensional heteronuclear NMR spectroscopy.
Protein Sci. 1995...
nmrlearner
Journal club
0
08-22-2010 03:41 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...