Probing the contribution of internal cavities to the volume change of protein unfolding under pressure (Q33368866)

26 July 2017

title

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

1 reference

26 July 2017

Frye KJ

1

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26 July 2017

Royer CA

series ordinal

2

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26 July 2017

publication date

1 October 1998

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26 July 2017

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26 July 2017

volume

7

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26 July 2017

issue

10

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26 July 2017

page(s)

2217-2222

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Detection, delineation, measurement and display of cavities in macromolecular structures

26 July 2017

cites work

1 reference

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Comparison of straight chain and cyclic unnatural amino acids embedded in the core of staphylococcal nuclease

21 June 2018

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The kinetic basis for the stabilization of staphylococcal nuclease by xylose

21 June 2018

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On volume changes accompanying conformational transitions of biopolymers

21 June 2018

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

21 June 2018

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Least activation path for protein folding: investigation of staphylococcal nuclease folding by stopped-flow circular dichroism

21 June 2018

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Pressure stability of proteins

21 June 2018

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High pressure effects on proteins and other biomolecules

21 June 2018

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Enzymes under extremes of physical conditions

21 June 2018

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The effect of high pressure upon proteins and other biomolecules

21 June 2018

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The interpretation of protein structures: Total volume, group volume distributions and packing density

21 June 2018

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Pressure denaturation of metmyoglobin

21 June 2018

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Structure volume relationships of proteins. Dilatometric studies of the structural transitions engendered in serum albumin and myoglobin as a consequence of acid-base reaction in water and in denaturing media

21 June 2018

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Genetic analysis of staphylococcal nuclease: identification of three intragenic "global" suppressors of nuclease-minus mutations

21 June 2018

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Internal cavities and buried waters in globular proteins.

21 June 2018

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Heme protein fluorescence versus pressure

21 June 2018

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21 June 2018

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Dominant forces in protein folding

21 June 2018

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Analysis of binding in macromolecular complexes: a generalized numerical approach

21 June 2018

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Fluorescence and conformational stability studies of Staphylococcus nuclease and its mutants, including the less stable nuclease-concanavalin A hybrids.

21 June 2018

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The crystal structure of staphylococcal nuclease refined at 1.7 A resolution

21 June 2018

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Kinetic analysis of the acid and the alkaline unfolded states of staphylococcal nuclease.

21 June 2018

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Numerical analysis of binding data: advantages, practical aspects, and implications

21 June 2018

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Response of a protein structure to cavity-creating mutations and its relation to the hydrophobic effect

21 June 2018

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High-resolution NMR study of the pressure-induced unfolding of lysozyme

21 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2143842

Thermodynamics of structural stability and cooperative folding behavior in proteins

21 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2143842

Areas, volumes, packing and protein structure

21 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2143842

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

21 June 2018

1 reference

Crossref

https://api.crossref.org/works/10.1002/PRO.5560071020

Pressure-induced reversible dissociation of enolase.

21 January 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2143842

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

31 October 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2143842

High-Pressure Denaturation of Staphylococcal Nuclease Proline-to-Glycine Substitution Mutants†

31 October 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2143842

Effects of denaturants at low concentrations on the reversible denaturation of staphylococcal nuclease

31 October 2018

1 reference

12 December 2020

pH-Induced folding/unfolding of staphylococcal nuclease: determination of kinetic parameters by the sequential-jump method

1 reference

12 December 2020

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

1 reference

12 December 2020

Reversible pressure-temperature denaturation of chymotrypsinogen

1 reference

12 December 2020

Mutant forms of staphylococcal nuclease with altered patterns of guanidine hydrochloride and urea denaturation

1 reference

12 December 2020

Energetics of denaturation and m values of staphylococcal nuclease mutants

1 reference

12 December 2020

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

1 reference

12 December 2020

Identifiers

DOI

10.1002/PRO.5560071020

1 reference

26 July 2017

1 reference

26 July 2017

1 reference