(Q73340034)

English

Relationships between conformation of beta-lactoglobulin in solution and gel states as revealed by attenuated total reflection Fourier transform infrared spectroscopy

scientific article published on 01 December 1999

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scholarly article

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3 November 2019

Relationships between conformation of beta-lactoglobulin in solution and gel states as revealed by attenuated total reflection Fourier transform infrared spectroscopy (English)

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3 November 2019

infrared spectroscopy

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A F Allain

1

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3 November 2019

P Paquin

2

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3 November 2019

M Subirade

3

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3 November 2019

publication date

1 December 1999

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3 November 2019

International Journal of Biological Macromolecules

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3 November 2019

26

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3 November 2019

5

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3 November 2019

337-344

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3 November 2019

Modifications occur at different structural levels during the heat denaturation of beta-lactoglobulin

1 reference

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Heat and cold denaturation of beta-lactoglobulin B

1 reference

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Structural and conformational changes of beta-lactoglobulin B: an infrared spectroscopic study of the effect of pH and temperature

1 reference

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Effects of physicochemical factors on the secondary structure of beta-lactoglobulin

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Conformation changes of beta-lactoglobulin: an ATR infrared spectroscopic study of the effect of pH and ethanol

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Effect of pressure on the deuterium exchange reaction of alpha-lactalbumin and beta-lactoglobulin

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Smoothing and Differentiation of Data by Simplified Least Squares Procedures

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Examination of the secondary structure of proteins by deconvolved FTIR spectra

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Manganese and calcium binding sites of concanavalin A

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Quantitative studies of the structure of proteins in solution by Fourier-transform infrared spectroscopy.

1 reference

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7 January 2021

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Reversible and irreversible modifications ofβ-lactoglobulin upon exposure to heat

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Solvent denaturation of proteins as observed by resolution-enhanced Fourier transform infrared spectroscopy

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Protective effect of lipidic surfaces against pressure-induced conformational changes of poly(L-lysine).

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Halogenated alcohols as solvents for proteins: FTIR spectroscopic studies.

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New insight into protein secondary structure from resolution-enhanced infrared spectra

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Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins

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Membrane binding induces destabilization of cytochrome c structure.

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7 January 2021

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Determination of the secondary structure content of proteins in aqueous solutions from their amide I and amide II infrared bands. Comparison between classical and partial least-squares methods.

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Protein secondary structures in water from second-derivative amide I infrared spectra

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Conformational changes upon dissociation of a globular protein from pea: a Fourier transform infrared spectroscopy study

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The structure of β-lactoglobulin and its similarity to plasma retinol-binding protein

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Bovine beta-lactoglobulin at 1.8 A resolution--still an enigmatic lipocalin

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Conformation of beta-Lactoglobulin Studied by FTIR: Effect of pH, Temperature, and Adsorption to the Oil-Water Interface.

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Pressure-induced change in proteins studied through chemical modifications

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Structure of pressure-induced denatured state of human serum albumin: a comparison with the intermediate in urea-induced denaturation

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Pressure-induced inactivation of E. coli beta-galactosidase: influence of pH and temperature.

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Effect of high hydrostatic pressure on the enzymic hydrolysis of beta-lactoglobulin B by trypsin, thermolysin and pepsin

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Identifiers

10.1016/S0141-8130(99)00104-X

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10628535%20AND%20SRC:MED&resulttype=core&format=json

3 November 2019

PubMed publication ID

1 reference

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PubMed publication ID

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3 November 2019

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