High-resolution nuclear magnetic resonance studies of proteins (Q34620041)

3 August 2017

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title

High-resolution nuclear magnetic resonance studies of proteins (English)

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3 August 2017

Jiri Jonas

1

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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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3 August 2017

number of pages

15

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Biochimica et Biophysica Acta

inferred from page(s)

published in

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3 August 2017

volume

1595

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3 August 2017

issue

1-2

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3 August 2017

page(s)

145-159

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The effect of high pressure upon proteins and other biomolecules

3 August 2017

cites work

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Nuclear magnetic resonance at high pressure

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High pressure effects on protein structure and function

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The use of hydrostatic pressure as a tool to study viruses and other macromolecular assemblages

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Intermediates in the folding reactions of small proteins

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The denatured state (the other half of the folding equation) and its role in protein stability.

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High-pressure NMR spectroscopy of proteins and membranes

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7 January 2021

High-resolution, high-pressure NMR studies of proteins

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A high-pressure, high-resolution NMR probe for experiments at 500 MHz.

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Molten-globule conformation of Arc repressor monomers determined by high-pressure 1H NMR spectroscopy.

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High-Pressure NMR Study of the Dissociation of Arc Repressor

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Rapid internal dynamics of BPTI is insensitive to pressure. (15)N spin relaxation at 2 kbar

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Pressure-induced changes in the folded structure of lysozyme

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The pressure-temperature free energy-landscape of staphylococcal nuclease monitored by (1)H NMR.

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Effect of pressure on individual hydrogen bonds in proteins. Basic pancreatic trypsin inhibitor

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Thermodynamics of unfolding of ribonuclease A under high pressure. A study by proton NMR

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Protein folding studied using hydrogen-exchange labeling and two-dimensional NMR

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7 January 2021

Structure of pressure-assisted cold denatured lysozyme and comparison with lysozyme folding intermediates

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Cold denaturation and 2H2O stabilization of a staphylococcal nuclease mutant

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7 January 2021

NMR Study of the Cold, Heat, and Pressure Unfolding of Ribonuclease A

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Hydrogen-exchange kinetics in the cold denatured state of ribonuclease A

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Nuclear magnetic resonance evidence for a structural intermediate at an early stage in the refolding of ribonuclease A

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Structure of very early protein folding intermediates: new insights through a variant of hydrogen exchange labelling

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Structure of the pressure-assisted cold denatured state of ubiquitin

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High-pressure denaturation of apomyoglobin

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Molecular mechanisms of acid denaturation. The role of histidine residues in the partial unfolding of apomyoglobin

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7 January 2021

Alternative models for describing the acid unfolding of the apomyoglobin folding intermediate

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7 January 2021

Structural and dynamic characterization of partially folded states of apomyoglobin and implications for protein folding

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7 January 2021

Structure and stability of a second molten globule intermediate in the apomyoglobin folding pathway

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7 January 2021

Discrete intermediates versus molten globule models for protein folding: characterization of partially folded intermediates of apomyoglobin

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7 January 2021

Effects of high pressure and temperature on the wild-type and F29W mutant forms of the N-domain of avian troponin C.

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7 January 2021

Properties of isolated recombinant N and C domains of chicken troponin C.

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Construction and characterization of a spectral probe mutant of troponin C: application to analyses of mutants with increased calcium affinity

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7 January 2021

A comparative spectroscopic study of tryptophan probes engineered into high- and low-affinity domains of recombinant chicken troponin C

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7 January 2021

Ca2+, Mg2+, and troponin I inhibitory peptide binding to a Phe-154 to Trp mutant of chicken skeletal muscle troponin C.

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7 January 2021

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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7 January 2021

10.1016/S0167-4838(01)00341-7

Identifiers

DOI

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3 August 2017

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