FTIR study on heat-induced and pressure-assisted cold-induced changes in structure of bovine alpha-lactalbumin: stabilizing role of calcium ion (Q73338862)

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scientific article published on 01 January 2001

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English	FTIR study on heat-induced and pressure-assisted cold-induced changes in structure of bovine alpha-lactalbumin: stabilizing role of calcium ion	scientific article published on 01 January 2001

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scholarly article

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3 November 2019

FTIR study on heat-induced and pressure-assisted cold-induced changes in structure of bovine alpha-lactalbumin: stabilizing role of calcium ion (English)

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3 November 2019

author name string

Dzwolak W

1

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3 November 2019

Kato M

2

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3 November 2019

Shimizu A

3

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3 November 2019

Taniguchi Y

4

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publication date

1 January 2001

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3 November 2019

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3 November 2019

62

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3 November 2019

1

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3 November 2019

29-39

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3 November 2019

Cold denaturation of proteins

1 reference

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21 January 2018

Ion pairs involved in maintaining a thermostable structure of glutamate dehydrogenase from a hyperthermophilic archaeon

1 reference

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21 January 2018

Protein thermostability above 100 degreesC: a key role for ionic interactions

1 reference

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21 January 2018

Do salt bridges stabilize proteins? A continuum electrostatic analysis.

1 reference

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21 January 2018

The stability of salt bridges at high temperatures: implications for hyperthermophilic proteins

1 reference

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21 January 2018

Structural adaptations of the cold-active citrate synthase from an Antarctic bacterium

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21 January 2018

Heat and cold denatured states of monomeric lambda repressor are thermodynamically and conformationally equivalent

1 reference

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21 January 2018

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

1 reference

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21 January 2018

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

1 reference

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21 January 2018

Cold denaturation and heat denaturation of Streptomyces subtilisin inhibitor. 1. CD and DSC studies

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21 January 2018

Characterization of the critical state in protein folding. Effects of guanidine hydrochloride and specific Ca2+ binding on the folding kinetics of alpha-lactalbumin

1 reference

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21 January 2018

Evidence for a molten globule state as a general intermediate in protein folding

1 reference

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21 January 2018

Molecular characterization of alpha-lactalbumin folding variants that induce apoptosis in tumor cells

1 reference

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21 January 2018

alpha-Lactalbumin: a calcium metalloprotein

1 reference

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21 January 2018

Refined structure of baboon α-lactalbumin at 1.7 Å resolution

1 reference

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21 January 2018

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

1 reference

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21 January 2018

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

1 reference

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21 January 2018

Functional identification of calcium binding residues in bovine alpha-lactalbumin

1 reference

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21 January 2018

Calorimetric determination of the energetics of the molten globule intermediate in protein folding: apo-alpha-lactalbumin

1 reference

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21 January 2018

Thermal unfolding of beta-lactoglobulin, alpha-lactalbumin, and bovine serum albumin. A thermodynamic approach

1 reference

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21 January 2018

A calorimetric study of the influence of calcium on the stability of bovine alpha-lactalbumin

1 reference

https://api.crossref.org/works/10.1002%2F1097-0282%282001%2962%3A1%3C29%3A%3AAID-BIP50%3E3.0.CO%3B2-A

21 January 2018

Cold denaturation of alpha-lactalbumin

1 reference

https://api.crossref.org/works/10.1002%2F1097-0282%282001%2962%3A1%3C29%3A%3AAID-BIP50%3E3.0.CO%3B2-A

21 January 2018

Diamond anvil cell and high-pressure physical investigations

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21 January 2018

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

1 reference

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21 January 2018

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

1 reference

https://api.crossref.org/works/10.1002%2F1097-0282%282001%2962%3A1%3C29%3A%3AAID-BIP50%3E3.0.CO%3B2-A

21 January 2018

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

1 reference

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21 January 2018

Cooperative thermal transitions of bovine and human apo-α-lactalbumins: evidence for a new intermediate state

1 reference

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21 January 2018

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

1 reference

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21 January 2018

Energetics of solvent and ligand-induced conformational changes in alpha-lactalbumin.

1 reference

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21 January 2018

Identifiers

10.1002/1097-0282(2001)62:1<29::AID-BIP50>3.0.CO;2-A

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1 reference

Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11135190%20AND%20SRC:MED&resulttype=core&format=json

3 November 2019

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