Fourier-transform infrared spectroscopy study of the pressure-induced changes in the structure of the bovine alpha-lactalbumin: the stabilizing role of the calcium ion (Q78122762)

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scientific article published on 01 August 1999

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English	Fourier-transform infrared spectroscopy study of the pressure-induced changes in the structure of the bovine alpha-lactalbumin: the stabilizing role of the calcium ion	scientific article published on 01 August 1999

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scholarly article

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11 December 2019

Fourier-transform infrared spectroscopy study of the pressure-induced changes in the structure of the bovine alpha-lactalbumin: the stabilizing role of the calcium ion (English)

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11 December 2019

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W Dzwolak

1

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11 December 2019

M Kato

2

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11 December 2019

A Shimizu

3

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11 December 2019

Y Taniguchi

4

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11 December 2019

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1 August 1999

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11 December 2019

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11

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Biochimica et Biophysica Acta

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11 December 2019

1433

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11 December 2019

1-2

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11 December 2019

45-55

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11 December 2019

Proteins under pressure. The influence of high hydrostatic pressure on structure, function and assembly of proteins and protein complexes

1 reference

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7 January 2021

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High pressure effects on protein structure and function

1 reference

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7 January 2021

based on heuristic

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Protein structure and dynamics at high pressure.

1 reference

https://api.crossref.org/works/10.1016%2FS0167-4838%2899%2900150-8

7 January 2021

based on heuristic

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alpha-Lactalbumin: a calcium metalloprotein

1 reference

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Refined structure of baboon α-lactalbumin at 1.7 Å resolution

1 reference

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7 January 2021

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Crystal structure of human α-lactalbumin at 1·7 Å resolution

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Crystal structures of guinea-pig, goat and bovine alpha-lactalbumin highlight the enhanced conformational flexibility of regions that are significant for its action in lactose synthase

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Functional identification of calcium binding residues in bovine alpha-lactalbumin

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FT-IR study of the Ca2+-binding to bovine alpha-lactalbumin. Relationships between the type of coordination and characteristics of the bands due to the Asp COO- groups in the Ca2+-binding site

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Fourier-transform infrared spectroscopic studies on the coordination of the side-chain COO- groups to Ca2+ in equine lysozyme

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Thermodynamics of thermal unfolding of bovine apo-alpha-lactalbumin

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Influence of Ca2+ binding on the structure and stability of bovine alpha-lactalbumin studied by circular dichroism and nuclear magnetic resonance spectra

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Temperature-induced changes in protein structures studied by Fourier transform infrared spectroscopy and global analysis

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Ca2+-induced alteration in the unfolding behavior of alpha-lactalbumin

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Unfolding of the molten globule state of alpha-lactalbumin studied by 1H NMR

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FTIR spectroscopic kinetic analysis of alkaline phosphatase under hyperbaric manipulation

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Infrared studies of interaction between metal ions and Ca(2+)-binding proteins. Marker bands for identifying the types of coordination of the side-chain COO- groups to metal ions in pike parvalbumin (pI = 4.10)

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Metal-ion binding and the molecular conformational properties of alpha lactalbumin

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Secondary structure and temperature-induced unfolding and refolding of ribonuclease T1 in aqueous solution. A Fourier transform infrared spectroscopic study.

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A comparison of infrared spectra of proteins in solution and crystalline forms

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Effect of metal ion binding on the secondary structure of bovine alpha-lactalbumin as examined by infrared spectroscopy

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Structure based prediction of protein folding intermediates

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The pressure-induced structural change of bovine alpha-lactalbumin as studied by a fluorescence hydrophobic probe

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