Structure and dynamics of a conformationally constrained nitroxide side chain and applications in EPR spectroscopy. - Wikidata - wikimedia - TriplyDB

Structure and dynamics of a conformationally constrained nitroxide side chain and applications in EPR spectroscopy.

Structure and dynamics of a conformationally constrained nitroxide side chain and applications in EPR spectroscopy.

http://www.wikidata.org/entity/Q35239853

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Use of electron paramagnetic resonance to solve biochemical problems Full Atom Simulations of Spin Label Conformations High Resolution Structure and Double Electron-Electron Resonance of the Zebrafish Voltage-dependent Anion Channel 2 Reveal an Oligomeric Population High-resolution crystal structure of spin labelled (T21R1) azurin from Pseudomonas aeruginosa: a challenging structural benchmark for in silico spin labelling algorithms Long-range distance measurements in proteins at physiological temperatures using saturation recovery EPR spectroscopy Stationary-phase EPR for exploring protein structure, conformation, and dynamics in spin-labeled proteins Rotameric preferences of a protein spin label at edge-strand β-sheet sites.Probing topology and dynamics of the second transmembrane domain (M2δ) of the acetyl choline receptor using magnetically aligned lipid bilayers (bicelles) and EPR spectroscopy.Mapping molecular flexibility of proteins with site-directed spin labeling: a case study of myoglobin.Structure and dynamics of an imidazoline nitroxide side chain with strongly hindered internal motion in proteins.Structural refinement from restrained-ensemble simulations based on EPR/DEER data: application to T4 lysozyme.Structural investigation of the transmembrane domain of KCNE1 in proteoliposomes Structural and energetic determinants of adhesive binding specificity in type I cadherins Visualizing transient dark states by NMR spectroscopy.ESR study of interfacial hydration layers of polypeptides in water-filled nanochannels and in vitrified bulk solvents.The double-histidine Cu²⁺-binding motif: a highly rigid, site-specific spin probe for electron spin resonance distance measurements.A nucleotide-independent cyclic nitroxide label for monitoring segmental motions in nucleic acids High-resolution helix orientation in actin-bound myosin determined with a bifunctional spin label.Simulating the distance distribution between spin-labels attached to proteins Site-directed spin labeling of proteins for distance measurements in vitro and in cells.A bifunctional spin label reports the structural topology of phospholamban in magnetically-aligned bicelles.CHARMM-GUI PDB manipulator for advanced modeling and simulations of proteins containing nonstandard residues.Conformationally trapping the actin-binding cleft of myosin with a bifunctional spin label The use of the Rx spin label in orientation measurement on proteins, by EPR.Conformational changes of the HsDHODH N-terminal Microdomain via DEER Spectroscopy.Restrained-ensemble molecular dynamics simulations based on distance histograms from double electron-electron resonance spectroscopy.Peptide-Membrane Interactions by Spin-Labeling EPR DEER EPR measurements for membrane protein structures via bifunctional spin labels and lipodisq nanoparticles Conformational selection and adaptation to ligand binding in T4 lysozyme cavity mutants.Organization of the mitochondrial apoptotic BAK pore: oligomerization of the BAK homodimers.Structural basis of lipid-driven conformational transitions in the KvAP voltage-sensing domain Technological advances in site-directed spin labeling of proteins.New developments in spin labels for pulsed dipolar EPR.The histone chaperones Vps75 and Nap1 form ring-like, tetrameric structures in solution.Site-Specific Internal Motions in GB1 Protein Microcrystals Revealed by 3D ²H-¹³C-¹³C Solid-State NMR Spectroscopy A triarylmethyl spin label for long-range distance measurement at physiological temperatures using T1 relaxation enhancement.Development of electron spin echo envelope modulation spectroscopy to probe the secondary structure of recombinant membrane proteins in a lipid bilayer.Pulsed EPR distance measurements in soluble proteins by site-directed spin labeling (SDSL).Elucidating a relationship between conformational sampling and drug resistance in HIV-1 protease.Symmetry-constrained analysis of pulsed double electron-electron resonance (DEER) spectroscopy reveals the dynamic nature of the KcsA activation gate.

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Structure and dynamics of a conformationally constrained nitroxide side chain and applications in EPR spectroscopy.

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2011 nî lūn-bûn

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2011 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

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2011 թվականի սեպտեմբերին հրատարակված գիտական հոդված

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2011年論文

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2011年論文

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Structure and dynamics of a co ...... lications in EPR spectroscopy.

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Proceedings of the National Academy of Sciences of the United States of America

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Structure and dynamics of a co ...... lications in EPR spectroscopy.

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Duilio Cascio

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Evan K Brooks

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Kálmán Hideg

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Mark R Fleissner

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Michael D Bridges

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Tamás Kálai

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P2860

Structural basis of the conversion of T4 lysozyme into a transglycosidase by reengineering the active site

Size versus polarizability in protein-ligand interactions: binding of noble gases within engineered cavities in phage T4 lysozyme

Structural determinants of nitroxide motion in spin-labeled proteins: Solvent-exposed sites in helix B of T4 lysozyme

Recognition dynamics up to microseconds revealed from an RDC-derived ubiquitin ensemble in solution

Analysis of the interaction between charged side chains and the alpha-helix dipole using designed thermostable mutants of phage T4 lysozyme

Structural origin of weakly ordered nitroxide motion in spin-labeled proteins

Site-directed spin labeling of a genetically encoded unnatural amino acid

Crystal structure of rat intestinal fatty-acid-binding protein. Refinement and analysis of the Escherichia coli-derived protein with bound palmitate

Coot: model-building tools for molecular graphics

PHENIX: building new software for automated crystallographic structure determination

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39

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Wayne L. Hubbell

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51631759

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21911399

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3182725

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