Effect of hydrostatic pressure on unfolding of alpha-lactalbumin: volumetric equivalence of the molten globule and unfolded state. - Wikidata - awgldk - TriplyDB

Effect of hydrostatic pressure on unfolding of alpha-lactalbumin: volumetric equivalence of the molten globule and unfolded state.

Effect of hydrostatic pressure on unfolding of alpha-lactalbumin: volumetric equivalence of the molten globule and unfolded state.

http://www.wikidata.org/entity/Q41972010

about

Elevated pressure improves the extraction and identification of proteins recovered from formalin-fixed, paraffin-embedded tissue surrogates High-pressure SAXS study of folded and unfolded ensembles of proteins Structural plasticity of staphylococcal nuclease probed by perturbation with pressure and pH.Pressure-induced molten globule state of human acetylcholinesterase: structural and dynamical changes monitored by neutron scattering.Improving the Proteomic Analysis of Archival Tissue by Using Pressure-Assisted Protein Extraction: A Mechanistic Approach.Pressure-induced unfolding of the molten globule of all-Ala alpha-lactalbumin.Pressure effect on denaturant-induced unfolding of hen egg white lysozyme.Partial phase diagram of aqueous bovine carbonic anhydrase: analyses of the pressure-dependent temperatures of the low- to physiological-temperature nondenaturational conformational change and of unfolding to the molten globule state.

P2860

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P2860

Effect of hydrostatic pressure on unfolding of alpha-lactalbumin: volumetric equivalence of the molten globule and unfolded state.

http://www.wikidata.org/entity/Q41972010

description

1999 nî lūn-bûn

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1999年の論文

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1999年論文

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1999年論文

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1999年論文

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1999年論文

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1999年論文

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1999年论文

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1999年论文

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1999年论文

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name

Effect of hydrostatic pressure ...... en globule and unfolded state.

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type

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Effect of hydrostatic pressure ...... en globule and unfolded state.

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Effect of hydrostatic pressure ...... en globule and unfolded state.

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Protein Science

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Effect of hydrostatic pressure ...... en globule and unfolded state.

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Kobashigawa Y

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Nitta K

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Sakurai M

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P2860

Crystal structures of the apo- and holomutant human lysozymes with an introduced Ca2+ binding site

Effect of the extra n-terminal methionine residue on the stability and folding of recombinant alpha-lactalbumin expressed in Escherichia coli

Some factors in the interpretation of protein denaturation

Principles that govern the folding of protein chains

How does a protein fold?

Stability of protein structure and hydrophobic interaction.

Contribution of hydration to protein folding thermodynamics. I. The enthalpy of hydration.

Energetics of protein structure.

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

Use of liquid hydrocarbon and amide transfer data to estimate contributions to thermodynamic functions of protein folding from the removal of nonpolar and polar surface from water.

P304

2765-2772

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scholarly article

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10.1110/PS.8.12.2765

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12

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8

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227656521

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10631994

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2144233

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