Conformational changes during the nanosecond-to-millisecond unfolding of ubiquitin. - Wikidata - awgldk - TriplyDB

Conformational changes during the nanosecond-to-millisecond unfolding of ubiquitin.

Conformational changes during the nanosecond-to-millisecond unfolding of ubiquitin.

http://www.wikidata.org/entity/Q30499610

about

His26 protonation in cytochrome c triggers microsecond β-sheet formation and heme exposure: implications for apoptosis Molecular basis for the structural stability of an enclosed β-barrel loop.Disulfide bond influence on protein structural dynamics probed with 2D-IR vibrational echo spectroscopy Mid-infrared spectroscopy for protein analysis: potential and challenges.Simulation study of chiral two-dimensional ultraviolet spectroscopy of the protein backbone.Computing infrared spectra of proteins using the exciton model Watching Proteins Wiggle: Mapping Structures with Two-Dimensional Infrared Spectroscopy.How to turn your pump-probe instrument into a multidimensional spectrometer: 2D IR and Vis spectroscopies via pulse shaping.Automated 2D IR spectroscopy using a mid-IR pulse shaper and application of this technology to the human islet amyloid polypeptide Transient two-dimensional IR spectrometer for probing nanosecond temperature-jump kinetics.Transient 2D IR spectroscopy of ubiquitin unfolding dynamics Temperature-dependent downhill unfolding of ubiquitin. I. Nanosecond-to-millisecond resolved nonlinear infrared spectroscopy.Fast photochemical oxidation of protein footprints faster than protein unfolding.Probing the structure of a rotaxane with two-dimensional infrared spectroscopy.Dissecting the mechanical unfolding of ubiquitin.Coherent femtosecond multidimensional probes of molecular vibrations.Sulfate radical anion as a new reagent for fast photochemical oxidation of proteins.Ultrafast 2D IR microscopy Coherent multidimensional optical spectroscopy of excitons in molecular aggregates; quasiparticle versus supermolecule perspectives.Laser-driven microsecond temperature cycles analyzed by fluorescence polarization microscopy.A transferable electrostatic map for solvation effects on amide I vibrations and its application to linear and two-dimensional spectroscopy.Power-law dependence of the melting temperature of ubiquitin on the volume fraction of macromolecular crowders.Amide vibrations are delocalized across the hydrophobic interface of a transmembrane helix dimer.Refolding upon force quench and pathways of mechanical and thermal unfolding of ubiquitin.Substrate binding and protein conformational dynamics measured by 2D-IR vibrational echo spectroscopy.Probing the folding transition state of ubiquitin mutants by temperature-jump-induced downhill unfolding.Protein folding and unfolding studied at atomic resolution by fast two-dimensional NMR spectroscopy Neuroglobin dynamics observed with ultrafast 2D-IR vibrational echo spectroscopy.Force-clamp analysis techniques give highest rank to stretched exponential unfolding kinetics in ubiquitin.Parallel β-sheet vibrational couplings revealed by 2D IR spectroscopy of an isotopically labeled macrocycle: quantitative benchmark for the interpretation of amyloid and protein infrared spectra.Atomic-level description of ubiquitin folding.Empirical amide I vibrational frequency map: application to 2D-IR line shapes for isotope-edited membrane peptide bundles.Native and unfolded cytochrome c--comparison of dynamics using 2D-IR vibrational echo spectroscopy.Structural disorder of the CD3zeta transmembrane domain studied with 2D IR spectroscopy and molecular dynamics simulations.Two-dimensional stimulated resonance Raman spectroscopy study of the Trp-cage peptide folding.2D IR provides evidence for mobile water molecules in beta-amyloid fibrils Dynamic localization of electronic excitation in photosynthetic complexes revealed with chiral two-dimensional spectroscopy.Microsecond molecular dynamics simulation of guanidinium chloride induced unfolding of ubiquitin.X-ray scattering experiments with high-flux X-ray source coupled rapid mixing microchannel device and their potential for high-flux neutron scattering investigations.Applications of 2D IR spectroscopy to peptides, proteins, and hydrogen-bond dynamics

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P2860

Conformational changes during the nanosecond-to-millisecond unfolding of ubiquitin.

http://www.wikidata.org/entity/Q30499610

description

2005 nî lūn-bûn

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2005 թուականի Յունուարին հրատարակուած գիտական յօդուած

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2005年の論文

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2005年論文

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2005年论文

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name

Conformational changes during the nanosecond-to-millisecond unfolding of ubiquitin.

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Conformational changes during the nanosecond-to-millisecond unfolding of ubiquitin.

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type

label

Conformational changes during the nanosecond-to-millisecond unfolding of ubiquitin.

@ast

Conformational changes during the nanosecond-to-millisecond unfolding of ubiquitin.

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prefLabel

Conformational changes during the nanosecond-to-millisecond unfolding of ubiquitin.

@ast

Conformational changes during the nanosecond-to-millisecond unfolding of ubiquitin.

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PNAS.0408646102

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

P1476

Conformational changes during the nanosecond-to-millisecond unfolding of ubiquitin

@en

P2093

Andrei Tokmakoff

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

Hoi Sung Chung

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Munira Khalil

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

P2860

Polymer principles and protein folding

Structure of ubiquitin refined at 1.8 A resolution

Theory of protein folding: the energy landscape perspective.

Helix formation via conformation diffusion search

Protein folding and unfolding on a complex energy landscape.

Absolute comparison of simulated and experimental protein-folding dynamics.

Fast kinetics and mechanisms in protein folding.

Characterization of a partially denatured state of a protein by two-dimensional NMR: reduction of the hydrophobic interactions in ubiquitin.

The fast protein folding problem.

Ultrafast thermally induced unfolding of RNase A

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612-617

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scholarly article

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10.1073/PNAS.0408646102

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102

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15630083

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