About: Effects of amino acid substitutions on the pressure denaturation of staphylococcal nuclease as monitored by fluorescence and nuclear magnetic resonance spectroscopy

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About: Effects of amino acid substitutions on the pressure denaturation of staphylococcal nuclease as monitored by fluorescence and nuclear magnetic resonance spectroscopy Goto Sponge NotDistinct Permalink

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scientific article published on 01 May 1993

Attributes	Values
rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована в травні 1993 (uk) im Mai 1993 veröffentlicher wissenschaftlicher Artikel (de) artículu científicu espublizáu en mayu de 1993 (ast) scientific article published on 01 May 1993 (en)
publication date	wds:Q70719533-93875D73-2EBE-4CD8-A8DC-E03F33DAFFBB
publication date	1993-05-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q70719533-4B63470D-39DE-4BD2-80D7-0D17A2D73F40
language of work or name	English
author name string	wds:Q70719533-0FB3D49A-B71F-42CA-8E26-2EB5778BF636 wds:Q70719533-3780571D-0739-4E53-9479-7F655532472E wds:Q70719533-5A61C004-4EB5-4C4C-859F-D7726B805821 wds:Q70719533-62D36491-7CBA-40AD-AC17-F6C4E1407570 wds:Q70719533-ABE93F84-86E3-4AC4-87D2-941DCFE251D2 wds:Q70719533-DB0A3CEF-BCBB-4C72-BD8B-E50672A3289F wds:Q70719533-F9142242-CEFE-4B10-99EA-0435FE6E61CA
author name string	X Peng A P Hinck K E Prehoda J L Markley C A Royer J Jonas S N Loh
rdfs:label	Effects of amino acid substitutions on the pressure denaturation of staphylococcal nuclease as monitored by fluorescence and nuclear magnetic resonance spectroscopy (en) Effects of amino acid substitutions on the pressure denaturation of staphylococcal nuclease as monitored by fluorescence and nuclear magnetic resonance spectroscopy (nl)
skos:prefLabel	Effects of amino acid substitutions on the pressure denaturation of staphylococcal nuclease as monitored by fluorescence and nuclear magnetic resonance spectroscopy (en) Effects of amino acid substitutions on the pressure denaturation of staphylococcal nuclease as monitored by fluorescence and nuclear magnetic resonance spectroscopy (nl)
name	Effects of amino acid substitutions on the pressure denaturation of staphylococcal nuclease as monitored by fluorescence and nuclear magnetic resonance spectroscopy (en) Effects of amino acid substitutions on the pressure denaturation of staphylococcal nuclease as monitored by fluorescence and nuclear magnetic resonance spectroscopy (nl)
title	wds:Q70719533-EFBD93FC-E2CD-4EBB-A77D-7EE683070C55
title	Effects of amino acid substitutions on the pressure denaturation of staphylococcal nuclease as monitored by fluorescence and nuclear magnetic resonance spectroscopy (en)
page(s)	wds:Q70719533-53112E1D-7C57-473B-839E-16017CFDE12E
page(s)	5222-5232
instance of	wds:Q70719533-5B403884-8E81-4CEA-9CFB-1CBC58601747
instance of	scholarly article
main subject	wds:Q70719533-9A7E5CBE-11AB-448F-B63D-254133EA6C60 wds:Q70719533-CCEFFA34-A768-405D-BD4D-E5CF9B6EC371
main subject	denaturation spectroscopy
PubMed ID	wds:Q70719533-6C1A1025-0111-4EC0-8579-9B884ED2C7E5
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/8494899
PubMed ID	8494899
published in	wds:Q70719533-3AD0B17A-A489-4EE7-8F70-A1804B3E0B1C
published in	Biochemistry
issue	wds:Q70719533-8B3F7056-0EFD-4331-9CA6-A375CBEC9487
volume	wds:Q70719533-9B19B77D-BA0E-4D98-A93A-26B9D93F60C2
issue	19
volume	32
DOI	wds:Q70719533-0BEDD8FB-D5C5-4575-997C-0268E2C28813
DOI	http://dx.doi.org/10.1021/BI00070A034
DOI	10.1021/BI00070A034
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q70719533
is cites work of	Tryptophan phosphorescence and pressure effects on protein structure. 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. Protein folding: independent unrelated pathways or predetermined pathway with optional errors The foldon substructure of staphylococcal nuclease Probing the contribution of internal cavities to the volume change of protein unfolding under pressure The use of fluorescence methods to monitor unfolding transitions in proteins Pressure denaturation of the bacteriophage P22 coat protein and its entropic stabilization in icosahedral shells Folding kinetics of staphylococcal nuclease studied by tryptophan engineering and rapid mixing methods Early formation of a beta hairpin during folding of staphylococcal nuclease H124L as detected by pulsed hydrogen exchange Solution structures of staphylococcal nuclease from multidimensional, multinuclear NMR: nuclease-H124L and its ternary complex with Ca2+ and thymidine-3',5'-bisphosphate Coupling between trans/cis proline isomerization and protein stability in staphylococcal nuclease High-resolution nuclear magnetic resonance studies of proteins Revisiting volume changes in pressure-induced protein unfolding. Determination of the volume changes for pressure-induced transitions of apomyoglobin between the native, molten globule, and unfolded states The use of hydrostatic pressure as a tool to study viruses and other macromolecular assemblages Protein Folding in the Absence of Chemical Denaturants On-line cell high-pressure nuclear magnetic resonance technique: application to protein studies Hydration of the folding transition state ensemble of a protein. Predicting the equilibrium protein folding pathway: structure-based analysis of staphylococcal nuclease Fluorescence characterization of Trp 21 in rat glutathione S-transferase 1-1: microconformational changes induced by S-hexyl glutathione The contribution of the residues from the main hydrophobic core of ribonuclease A to its pressure-folding transition state. Rapid internal dynamics of BPTI is insensitive to pressure. (15)N spin relaxation at 2 kbar Folding intermediates of a model three-helix bundle protein. Pressure and cold denaturation studies The kinetic basis for the stabilization of staphylococcal nuclease by xylose Thermodynamics of protein unfolding: questions pertinent to testing the validity of the two-state model. Monitoring Hydrogen Exchange During Protein Folding by Fast Pressure Jump NMR Spectroscopy Effects of relative humidity and applied force on atomic force microscopy images of the filamentous phage fd P22 phage capsids under pressure Structure-relaxation mechanism for the response of T4 lysozyme cavity mutants to hydrostatic pressure Diversity in transcripts and translational pattern of stress proteins in marine extremophiles Study of protein folding under native conditions by rapidly switching the hydrostatic pressure inside an NMR sample cell. Monitoring 15N Chemical Shifts During Protein Folding by Pressure-Jump NMR Interrupted Pressure-Jump NMR Experiments Reveal Resonances of On-Pathway Protein Folding Intermediate Single-point amino acid substitutions at the 119th residue of thermolysin and their pressure-induced activation Pressure versus temperature unfolding of ribonuclease A: an FTIR spectroscopic characterization of 10 variants at the carboxy-terminal site Effect of hydrostatic pressure on the fluorescence of indole derivatives. A discussion of the physical basis for the pressure unfolding of proteins Lessons from pressure denaturation of proteins Niche specific amino acid features within the core genes of the genus Shewanella Protein structural changes characterized by high-pressure, pulsed field gradient diffusion NMR spectroscopy
is cites work of	wds:Q27747584-1902B5C3-750D-4B73-AE80-B10F08A0B46E wds:Q30167733-4B586597-C718-4AB0-9E10-3D3CC93A6101 wds:Q41052911-21DE4D93-F7F6-4613-B91D-1897D1588954 wds:Q73561344-1CB57D83-E3B2-4F6C-8015-93D6D9727A56 wds:Q30330244-77E000EA-07F8-4785-93FB-8809D5CE40B7 wds:Q30158038-AB2EF769-016E-49C3-86C2-70FD0E9C7D1B

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