Revisiting volume changes in pressure-induced protein unfolding. (Q34620061)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11983396%20AND%20SRC:MED&resulttype=core&format=json

10 December 2019

review article

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title

Revisiting volume changes in pressure-induced protein unfolding (English)

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11983396%20AND%20SRC:MED&resulttype=core&format=json

10 December 2019

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11983396%20AND%20SRC:MED&resulttype=core&format=json

10 December 2019

Catherine A Royer

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3 August 2017

language of work or name

English

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publication date

1 March 2002

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11983396%20AND%20SRC:MED&resulttype=core&format=json

Biochimica et Biophysica Acta

10 December 2019

published in

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11983396%20AND%20SRC:MED&resulttype=core&format=json

10 December 2019

volume

1595

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10 December 2019

issue

1-2

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10 December 2019

page(s)

201-209

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Thermodynamics of protein denaturation. Effect of pressure on the denaturation on ribonuclease A

10 December 2019

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The pressure dependence of hydrophobic interactions is consistent with the observed pressure denaturation of proteins.

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Some factors in the interpretation of protein denaturation

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Reversible pressure-temperature denaturation of chymotrypsinogen

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Evidence for a molten globule-like transition state in protein folding from determination of activation volumes

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Denaturant-induced movement of the transition state of protein folding revealed by high-pressure stopped-flow measurements

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STUDIES ON TAKA-AMYLASE A UNDER HIGH PRESSURE. 1. SOME KINETIC ASPECTS OF PRESSURE INACTIVATION OF TAKA-AMYLASE A.

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INFLUENCE OF PRESSURE ON THE REVERSIBLE UNFOLDING OR RIBONUCLEASE AND POLY-GAMMA-L-GLUTAMATE

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Plurality of pressure-denatured forms in chymotrypsinogen and lysozyme

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Crystal structure of hen egg-white lysozyme at a hydrostatic pressure of 1000 atmospheres

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Pressure-induced changes in the folded structure of lysozyme

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Low-lying excited states of proteins revealed from nonlinear pressure shifts in 1H and 15N NMR.

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Pressure effects on protein secondary structure and hydrogen deuterium exchange in chymotrypsinogen: a Fourier transform infrared spectroscopic study

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Pressure- and thermally-induced reversible changes in the secondary structure of ribonuclease A studied by FT-IR spectroscopy

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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

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Differences between the pressure- and temperature-induced denaturation and aggregation of beta-lactoglobulin A, B, and AB monitored by FT-IR spectroscopy and small-angle X-ray scattering

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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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High-pressure effects on beta-lactoglobulin interactions with ligands studied by fluorescence

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Pressure-induced perturbation of apomyoglobin structure: fluorescence studies on native and acidic compact forms

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Pressure-induced perturbation of ANS-apomyoglobin complex: frequency domain fluorescence studies on native and acidic compact states

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Testing the correlation between delta A and delta V of protein unfolding using m value mutants of staphylococcal nuclease.

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The kinetic basis for the stabilization of staphylococcal nuclease by xylose

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Determination of the volume changes for pressure-induced transitions of apomyoglobin between the native, molten globule, and unfolded states

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Probing the contribution of internal cavities to the volume change of protein unfolding under pressure

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Single-point amino acid substitutions at the 119th residue of thermolysin and their pressure-induced activation

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Identifiers

DOI

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10 December 2019

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