Determination of the solution structure of Apo calbindin D9k by NMR spectroscopy
about
The EF-hand domain: a globally cooperative structural unitAn extended hudrophobic core induces EF-hand swappingSolution Structure of the Apo C-Terminal Domain of the Lethocerus F1 Troponin C IsoformStructure of the Small Dictyostelium discoideum Myosin Light Chain MlcB Provides Insights into MyoB IQ Motif RecognitionSolution NMR structures of the C-domain of Tetrahymena cytoskeletal protein Tcb2 reveal distinct calcium-induced structural rearrangementsThe structure of calcyclin reveals a novel homodimeric fold for S100 Ca(2+)-binding proteinsSolution structure of the Eps15 homology domain of a human POB1 (partner of RalBP1)A model for target protein binding to calcium-activated S100 dimersSolvation energetics and conformational change in EF-hand proteinsA united residue force-field for calcium-protein interactions.Improvement of the treatment of loop structures in the UNRES force field by inclusion of coupling between backbone- and side-chain-local conformational states.An improved functional form for the temperature scaling factors of the components of the mesoscopic UNRES force field for simulations of protein structure and dynamics.A calbindin D9k mutant containing a novel structural extension: 1H nuclear magnetic resonance studies.The heterodimeric complex of MRP-8 (S100A8) and MRP-14 (S100A9). Antibody recognition, epitope definition and the implications for structure.Diversity of conformational states and changes within the EF-hand protein superfamily.Combining conformational flexibility and continuum electrostatics for calculating pK(a)s in proteins.Relating form and function of EF-hand calcium binding proteins.Physics-based potentials for the coupling between backbone- and side-chain-local conformational states in the UNited RESidue (UNRES) force field for protein simulations.Characterization of the N-terminal half-saturated state of calbindin D9k: NMR studies of the N56A mutant.An interaction-based analysis of calcium-induced conformational changes in Ca2+ sensor proteinsTwo novel mitochondrial and chloroplastic targeting-peptide-degrading peptidasomes in A. thaliana, AtPreP1 and AtPreP2.Structure of Guanylyl Cyclase Activator Protein 1 (GCAP1) Mutant V77E in a Ca2+-free/Mg2+-bound Activator State.Energy-based de novo protein folding by conformational space annealing and an off-lattice united-residue force field: application to the 10-55 fragment of staphylococcal protein A and to apo calbindin D9K.Structure and dynamics of Ca2+-binding domain 1 of the Na+/Ca2+ exchanger in the presence and in the absence of Ca2+Converting a protein into a switch for biosensing and functional regulation.Protein conformational switches: from nature to design.Multiscale characterization of protein conformational ensemblesChemical shift assignments of the C-terminal Eps15 homology domain-3 EH domain.Structural basis for the negative allostery between Ca(2+)- and Mg(2+)-binding in the intracellular Ca(2+)-receptor calbindin D9kA Ca2+-sensing molecular switch based on alternate frame protein folding.Identification of the binding site on S100B protein for the actin capping protein CapZ.TSAR: a program for automatic resonance assignment using 2D cross-sections of high dimensionality, high-resolution spectra.Focusing of the electrostatic potential at EF-hands of calbindin D(9k): titration of acidic residues.Coupling of ligand binding and dimerization of helix-loop-helix peptides: spectroscopic and sedimentation analyses of calbindin D9k EF-hands.Evidence for the involvement of the unique C-tail of S100A9 in the binding of arachidonic acid to the heterocomplex S100A8/A9.Global and local Voronoi analysis of solvation shells of proteins.Modern protein force fields behave comparably in molecular dynamics simulations.NMR investigation and secondary structure of domains I and II of rat brain calbindin D28k (1-93).Reduced dimensionality (3,2)D NMR experiments and their automated analysis: implications to high-throughput structural studies on proteins.Intrinsic disorder in S100 proteins.
P2860
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P2860
Determination of the solution structure of Apo calbindin D9k by NMR spectroscopy
description
1995 nî lūn-bûn
@nan
1995 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի հունիսին հրատարակված գիտական հոդված
@hy
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
name
Determination of the solution structure of Apo calbindin D9k by NMR spectroscopy
@ast
Determination of the solution structure of Apo calbindin D9k by NMR spectroscopy
@en
Determination of the solution structure of Apo calbindin D9k by NMR spectroscopy
@nl
type
label
Determination of the solution structure of Apo calbindin D9k by NMR spectroscopy
@ast
Determination of the solution structure of Apo calbindin D9k by NMR spectroscopy
@en
Determination of the solution structure of Apo calbindin D9k by NMR spectroscopy
@nl
prefLabel
Determination of the solution structure of Apo calbindin D9k by NMR spectroscopy
@ast
Determination of the solution structure of Apo calbindin D9k by NMR spectroscopy
@en
Determination of the solution structure of Apo calbindin D9k by NMR spectroscopy
@nl
P2093
P356
P1476
Determination of the solution structure of Apo calbindin D9k by NMR spectroscopy
@en
P2093
P304
P356
10.1006/JMBI.1995.0308
P407
P577
1995-06-02T00:00:00Z