Steady-state and transient ultraviolet resonance Raman spectrometer for the 193-270 nm spectral region. - Wikidata - wikimedia - TriplyDB

Steady-state and transient ultraviolet resonance Raman spectrometer for the 193-270 nm spectral region.

Steady-state and transient ultraviolet resonance Raman spectrometer for the 193-270 nm spectral region.

http://www.wikidata.org/entity/Q33230778

about

UV resonance Raman investigations of peptide and protein structure and dynamics Insights into Protein Structure and Dynamics by Ultraviolet and Visible Resonance Raman Spectroscopy Glutamine and Asparagine Side Chain Hyperconjugation-Induced Structurally Sensitive Vibrations.Elucidating Peptide and Protein Structure and Dynamics: UV Resonance Raman Spectroscopy.Sodium dodecyl sulfate monomers induce XAO peptide polyproline II to α-helix transition.Protein dynamics from time resolved UV Raman spectroscopy Identification of explosives with two-dimensional ultraviolet resonance Raman spectroscopy.UV resonance Raman determination of molecular mechanism of poly(N-isopropylacrylamide) volume phase transition.Lowest energy electronic transition in aqueous Cl(-) salts: Cl(-) → (H2O)6 charge transfer transition Note: deep ultraviolet Raman spectrograph with the laser excitation line down to 177.3 nm and its application.Direct observations of conformational distributions of intrinsically disordered p53 peptides using UV Raman and explicit solvent simulations Compact Solid-State 213 nm Laser Enables Standoff Deep Ultraviolet Raman Spectrometer: Measurements of Nitrate Photochemistry.Evolution of quantitative methods in protein secondary structure determination via deep-ultraviolet resonance Raman spectroscopy.Hydrogen bonding and solvent polarity markers in the uv resonance raman spectrum of tryptophan: application to membrane proteins.Circular dichroism and UV resonance raman study of the impact of alcohols on the Gibbs free energy landscape of an alpha-helical peptide.UV resonance Raman studies of the NaClO4 dependence of poly-L-lysine conformation and hydrogen exchange kinetics.Raman studies of solution polyglycine conformations.UV resonance Raman investigation of the conformations and lowest energy allowed electronic excited states of tri- and tetraalanine: charge transfer transitions.UV resonance Raman investigation of the aqueous solvation dependence of primary amide vibrations.Impact of ion binding on poly-L-lysine (un)folding energy landscape and kinetics.Circular dichroism and ultraviolet resonance Raman indicate little Arg-Glu side chain α-helix peptide stabilization UV resonance Raman finds peptide bond-Arg side chain electronic interactions Dependence of the AmII'p proline Raman band on peptide conformation Conformation of poly-L-glutamate is independent of ionic strength.UV resonance Raman spectroscopy monitors polyglutamine backbone and side chain hydrogen bonding and fibrillization Circular dichroism and UV-resonance Raman investigation of the temperature dependence of the conformations of linear and cyclic elastin.UV resonance raman investigation of electronic transitions in alpha-helical and polyproline II-like conformations Salt dependence of an alpha-helical peptide folding energy landscapes.UV Resonance Raman Elucidation of the Terminal and Internal Peptide Bond Conformations of Crystalline and Solution Oligoglycines.Ultraviolet resonance Raman study of side chain electrostatic control of poly-L-lysine conformation.UV resonance Raman and DFT studies of arginine side chains in peptides: insights into arginine hydration.Deep ultraviolet resonance Raman excitation enables explosives detection.High-throughput, high-resolution Echelle deep-UV Raman spectrometer.Deep-ultraviolet (UV) resonance raman spectroscopy as a tool for quality control of formulated therapeutic proteins.Solution and Solid Hexahydro-1,3,5-trinitro-1,3,5-triazine (RDX) Ultraviolet (UV) 229 nm Photochemistry.Solution and solid trinitrotoluene (TNT) photochemistry: persistence of TNT-like ultraviolet (UV) resonance Raman bands

P2860

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P2860

Steady-state and transient ultraviolet resonance Raman spectrometer for the 193-270 nm spectral region.

http://www.wikidata.org/entity/Q33230778

description

2005 nî lūn-bûn

@nan

2005 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2005 թվականի դեկտեմբերին հրատարակված գիտական հոդված

@hy

2005年の論文

@ja

2005年論文

@yue

2005年論文

@zh-hant

2005年論文

@zh-hk

2005年論文

@zh-mo

2005年論文

@zh-tw

2005年论文

@wuu

name

Steady-state and transient ult ...... he 193-270 nm spectral region.

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Steady-state and transient ult ...... he 193-270 nm spectral region.

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type

label

Steady-state and transient ult ...... he 193-270 nm spectral region.

@ast

Steady-state and transient ult ...... he 193-270 nm spectral region.

@en

prefLabel

Steady-state and transient ult ...... he 193-270 nm spectral region.

@ast

Steady-state and transient ult ...... he 193-270 nm spectral region.

@en

P1433

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000370205775142511

P1433

Applied Spectroscopy

P1476

Steady-state and transient ult ...... he 193-270 nm spectral region.

@en

P2093

Aleksandr Mikhonin

http://www.w3.org/2001/XMLSchema#string

Anatoli Ianoul

http://www.w3.org/2001/XMLSchema#string

Calum Munro

http://www.w3.org/2001/XMLSchema#string

Igor Lednev

http://www.w3.org/2001/XMLSchema#string

Sanford A Asher

http://www.w3.org/2001/XMLSchema#string

Sergei Bykov

http://www.w3.org/2001/XMLSchema#string

P2860

Catalytic and structural role of a metal-free histidine residue in bovine Cu-Zn superoxide dismutase.

Deep-UV Raman spectrometer tunable between 193 and 205 nm for structural characterization of proteins.

Probing protein structure and dynamics with resonance Raman spectroscopy: cytochrome c peroxidase and hemoglobin.

Protein structure from ultraviolet resonance Raman spectroscopy.

Protein conformation change of myoglobin upon ligand binding probed by ultraviolet resonance Raman spectroscopy.

Transient UV Raman spectroscopy finds no crossing barrier between the peptide alpha-helix and fully random coil conformation.

Helix formation via conformation diffusion search

Picosecond dynamics of G-protein coupled receptor activation in rhodopsin from time-resolved UV resonance Raman spectroscopy.

Structure and organization of bacteriophage Pf3 probed by Raman and ultraviolet resonance Raman spectroscopy.

UV Raman demonstrates that alpha-helical polyalanine peptides melt to polyproline II conformations.

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1541-1552

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scholarly article

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10.1366/000370205775142511

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12

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59

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2005-12-01T00:00:00Z

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P5875

7380026

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P698

16390595

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