About: Structural characterization of the pressure-denatured state and unfolding/refolding kinetics of staphylococcal nuclease by synchrotron small-angle X-ray scattering and Fourier-transform infrared spectroscopy 1 1Edited by P. E. Wright

Facets (new session)
Description
Metadata
Settings
- owl:sameAs
- Inference Rule:

About: Structural characterization of the pressure-denatured state and unfolding/refolding kinetics of staphylococcal nuclease by synchrotron small-angle X-ray scattering and Fourier-transform infrared spectroscopy 1 1Edited by P. E. Wright Goto Sponge NotDistinct Permalink

An Entity of Type : wikibase:Item, within Data Space : wikidata.demo.openlinksw.com associated with source document(s)

article

Attributes	Values
rdf:type	Item
description	article (en) wetenschappelijk artikel (nl) наукова стаття, опублікована в січні 1998 (uk) im Januar 1998 veröffentlichter wissenschaftlicher Artikel (de)
publication date	wds:Q57710414-93847B22-3497-4770-907F-A167CA775C04
publication date	1998-01-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q57710414-53428ACC-BF87-459C-AD1A-9C98FAE56976
language of work or name	English
author name string	wds:Q57710414-43CC85AC-E7F2-4CE3-8392-2B38D5EC4A92 wds:Q57710414-ACA8E9A4-3F14-4E4F-A312-ADF7FA954F7B wds:Q57710414-CAF409C1-FE04-4750-ABEB-F18B1B8F9C39 wds:Q57710414-E8E71472-743C-46F2-9004-8E444C1C508F
author name string	Rapp G Malessa R Panick G Frye KJ
rdfs:label	Structural characterization of the pressure-denatured state and unfolding/refolding kinetics of staphylococcal nuclease by synchrotron small-angle X-ray scattering and Fourier-transform infrared spectroscopy 1 1Edited by P. E. Wright (en) Structural characterization of the pressure-denatured state and unfolding/refolding kinetics of staphylococcal nuclease by synchrotron small-angle X-ray scattering and Fourier-transform infrared spectroscopy 1 1Edited by P. E. Wright (nl)
skos:prefLabel	Structural characterization of the pressure-denatured state and unfolding/refolding kinetics of staphylococcal nuclease by synchrotron small-angle X-ray scattering and Fourier-transform infrared spectroscopy 1 1Edited by P. E. Wright (en) Structural characterization of the pressure-denatured state and unfolding/refolding kinetics of staphylococcal nuclease by synchrotron small-angle X-ray scattering and Fourier-transform infrared spectroscopy 1 1Edited by P. E. Wright (nl)
name	Structural characterization of the pressure-denatured state and unfolding/refolding kinetics of staphylococcal nuclease by synchrotron small-angle X-ray scattering and Fourier-transform infrared spectroscopy 1 1Edited by P. E. Wright (en) Structural characterization of the pressure-denatured state and unfolding/refolding kinetics of staphylococcal nuclease by synchrotron small-angle X-ray scattering and Fourier-transform infrared spectroscopy 1 1Edited by P. E. Wright (nl)
author	wds:Q57710414-091F6499-8B4E-4B63-A426-85E33FED937C wds:Q57710414-AA17FC0F-EDE8-4EF9-95F3-C3D04F2ED299
author	Roland Winter Catherine A. Royer
title	wds:Q57710414-C8BB3100-1D48-48F4-86AA-C08D6D37A73F
title	Structural characterization of the pressure-denatured state and unfolding/refolding kinetics of staphylococcal nuclease by synchrotron small-angle X-ray scattering and Fourier-transform infrared spectroscopy (en)
page(s)	wds:Q57710414-83D45810-893D-47F3-8D44-D702329BB98E
page(s)	389-402
instance of	wds:Q57710414-E2E67D9F-77AC-453B-8C14-EB30FC5F1F3A
instance of	scholarly article
main subject	wds:Q57710414-15D43204-0003-41E2-886D-18A0F07A08BC wds:Q57710414-97D53670-7362-4E55-B471-2661466AB28A wds:Q57710414-9EEDBEB6-3F8E-429D-BD3F-47E36EEE3A64 wds:Q57710414-CA8178FC-A67E-443A-AD60-76851125A8BB
main subject	spectroscopy X-ray scattering techniques infrared spectroscopy refolding
PubMed ID	wds:Q57710414-86674B15-152C-435A-ADD8-0044CCBE3509
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/9466917
PubMed ID	9466917
published in	wds:Q57710414-7FE31EDF-990D-41A0-825D-DA50171D8283
published in	Journal of Molecular Biology
issue	wds:Q57710414-386ABB38-3755-42A0-905D-3C5A4B3BABBD
volume	wds:Q57710414-8714748B-A078-4511-83F5-3761997D3AD2
issue	2
volume	275
DOI	wds:Q57710414-936A4079-E9C5-49E2-AE55-9EC6C4AFE3BE
DOI	http://dx.doi.org/10.1006/JMBI.1997.1454
DOI	10.1006/JMBI.1997.1454
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q57710414
is cites work of	The C-terminal domain of the measles virus nucleoprotein is intrinsically disordered and folds upon binding to the C-terminal moiety of the phosphoprotein Expanding the pressure technique: insights into protein folding from combined use of pressure and chemical denaturants. Pressure response of protein backbone structure. Pressure-induced amide 15N chemical shifts in BPTI. Synchrotron X-ray and neutron small-angle scattering of lyotropic lipid mesophases, model biomembranes and proteins in solution at high pressure. Revealing conformational substates of lipidated N-Ras protein by pressure modulation The energy landscape theory of protein folding: insights into folding mechanisms and scenarios Early events in protein folding Probing the contribution of internal cavities to the volume change of protein unfolding under pressure Pressure denaturation of staphylococcal nuclease studied by neutron small-angle scattering and molecular simulation Comparative Fourier transform infrared spectroscopy study of cold-, pressure-, and heat-induced unfolding and aggregation of myoglobin Single-domain antibody fragments with high conformational stability Effect of molecular crowding on the temperature-pressure stability diagram of ribonuclease A Partial molar volume, surface area, and hydration changes for equilibrium unfolding and formation of aggregation transition state: high-pressure and cosolute studies on recombinant human IFN-gamma High-pressure 1H NMR study of pressure-induced structural changes in the heme environments of metcyanomyoglobins Folding and unfolding of an elastinlike oligopeptide: "inverse temperature transition," reentrance, and hydrogen-bond dynamics. Toward a taxonomy of the denatured state: small angle scattering studies of unfolded proteins Kinetic and thermodynamic characterization of dihydrotestosterone-induced conformational perturbations in androgen receptor ligand-binding domain The C-terminal domain of measles virus nucleoprotein belongs to the class of intrinsically disordered proteins that fold upon binding to their physiological partner New perspectives on hydrophobic effects High pressure simulations of biomolecules Revisiting volume changes in pressure-induced protein unfolding. Folding of a pressure-denatured model protein Electrospray ionization mass spectrometry as a method for studying the high-pressure denaturation of proteins Water Determines the Structure and Dynamics of Proteins Determination of the volume changes for pressure-induced transitions of apomyoglobin between the native, molten globule, and unfolded states Protein Folding in the Absence of Chemical Denaturants Impact of hydrostatic pressure on an intrinsically disordered protein: a high-pressure NMR study of α-synuclein Pressure provides new insights into protein folding, dynamics and structure Structural and thermodynamic characterization of T4 lysozyme mutants and the contribution of internal cavities to pressure denaturation High pressure NMR study of a small protein, gurmarin Structural plasticity of staphylococcal nuclease probed by perturbation with pressure and pH. Pressure-jump small-angle x-ray scattering detected kinetics of staphylococcal nuclease folding Effect of osmolytes on pressure-induced unfolding of proteins: a high-pressure SAXS study Toward resolution of ambiguity for the unfolded state. Simulations of the pressure and temperature unfolding of an alpha-helical peptide. Fourier transform infrared spectroscopy in high-pressure studies on proteins Towards an Understanding of the Temperature/ Pressure Configurational and Free-Energy Landscape of Biomolecules Effect of pressure on thermal stability of g-quadruplex DNA and double-stranded DNA structures Characterization of the temperature- and pressure-induced inverse and reentrant transition of the minimum elastin-like polypeptide GVG(VPGVG) by DSC, PPC, CD, and FT-IR spectroscopy Misplaced helix slows down ultrafast pressure-jump protein folding Pressure-A Gateway to Fundamental Insights into Protein Solvation, Dynamics, and Function. Characterization of the pressure-induced intermediate and unfolded state of red-shifted green fluorescent protein--a static and kinetic FTIR, UV/VIS and fluorescence spectroscopy study. Rapid internal dynamics of BPTI is insensitive to pressure. (15)N spin relaxation at 2 kbar High-pressure denaturation of apomyoglobin A sub-ms pressure jump setup for time-resolved X-ray scattering. Pressure-induced protein-folding/unfolding kinetics

Faceted Search & Find service v1.16.117 as of May 05 2024

Alternative Linked Data Documents: ODE Content Formats:

RDF

ODATA

Microdata

About

OpenLink Virtuoso version 07.20.3239 as of May 5 2024, on Linux (x86_64-centos_6-linux-gnu), Single-Server Edition (378 GB total memory, 180 GB memory in use)
Data on this page belongs to its respective rights holders.
Virtuoso Faceted Browser Copyright © 2009-2025 OpenLink Software