Literature DB >> 8060488

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

E Dufour1, P Robert, D Bertrand, T Haertlé.   

Abstract

Fourier transform infrared spectroscopy has been applied to investigate the secondary structural changes of beta-lactoglobulin in water/ethanol mixtures. The studies were carried out at two different pHs and at high protein concentrations. The spectra were recorded using an attenuated total reflection cell. The amide I band of beta-lactoglobulin in water reveals large amounts of intra extended beta-sheet structure. About 20% ethanol, beta-lactoglobulin unfolds and beta-strand formation is observed. alpha-Helices are built up by increasing the ethanol concentration up to 30%. In 50% ethanol, beta-lactoglobulin gels providing the apparent pH are neutral. The secondary structural changes of beta-lactoglobulin were observed on the similarity maps obtained by Principal Component Analysis.

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Year:  1994        PMID： 8060488     DOI： 10.1007/bf01891973

Source DB:  PubMed          Journal:  J Protein Chem        ISSN： 0277-8033


  20 in total

1.  Alcohol-induced changes of beta-lactoglobulin-retinol-binding stoichiometry.

Authors:  E Dufour; T Haertlé
Journal:  Protein Eng       Date:  1990-12

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

Authors:  H L Casal; U Köhler; H H Mantsch
Journal:  Biochim Biophys Acta       Date:  1988-11-02

3.  Crystal structure of the trigonal form of bovine beta-lactoglobulin and of its complex with retinol at 2.5 A resolution.

Authors:  H L Monaco; G Zanotti; P Spadon; M Bolognesi; L Sawyer; E E Eliopoulos
Journal:  J Mol Biol       Date:  1987-10-20       Impact factor: 5.469

Review 4.  New insight into protein secondary structure from resolution-enhanced infrared spectra.

Authors:  W K Surewicz; H H Mantsch
Journal:  Biochim Biophys Acta       Date:  1988-01-29

5.  Multivariate analysis applied to near-infrared spectra of milk.

Authors:  P Robert; D Bertrand; M F Devaux; R Grappin
Journal:  Anal Chem       Date:  1987-09-01       Impact factor: 6.986

6.  The enhancement of fluorescence and the decreased susceptibility to enzymatic oxidation of retinol complexed with bovine serum albumin, -lactoglobulin, and the retinol-binding protein of human plasma.

Authors:  S Futterman; J Heller
Journal:  J Biol Chem       Date:  1972-08-25       Impact factor: 5.157

7.  'Molten-globule state': a compact form of globular proteins with mobile side-chains.

Authors:  M Ohgushi; A Wada
Journal:  FEBS Lett       Date:  1983-11-28       Impact factor: 4.124

8.  Dissociation of beta-lactoglobulin near neutral pH.

Authors:  J K Zimmerman; G H Barlow; I M Klotz
Journal:  Arch Biochem Biophys       Date:  1970-05       Impact factor: 4.013

9.  The structure of beta-lactoglobulin and its similarity to plasma retinol-binding protein.

Authors:  M Z Papiz; L Sawyer; E E Eliopoulos; A C North; J B Findlay; R Sivaprasadarao; T A Jones; M E Newcomer; P J Kraulis
Journal:  Nature       Date:  1986 Nov 27-Dec 3       Impact factor: 49.962

10.  Halogenated alcohols as solvents for proteins: FTIR spectroscopic studies.

Authors:  M Jackson; H H Mantsch
Journal:  Biochim Biophys Acta       Date:  1992-01-09
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  2 in total

Review 1.  Intrinsically disordered proteins and their environment: effects of strong denaturants, temperature, pH, counter ions, membranes, binding partners, osmolytes, and macromolecular crowding.

Authors:  Vladimir N Uversky
Journal:  Protein J       Date:  2009-10       Impact factor: 2.371

2.  Interaction of curcumin and diacetylcurcumin with the lipocalin member beta-lactoglobulin.

Authors:  Fakhrossadat Mohammadi; Abdol-Khalegh Bordbar; Adeleh Divsalar; Khosro Mohammadi; Ali Akbar Saboury
Journal:  Protein J       Date:  2009-05       Impact factor: 2.371
  2 in total

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