Literature DB >> 8601463

Partially folded structure of monomeric bovine beta-lactoglobulin.

H Molinari1, L Ragona, L Varani, G Musco, R Consonni, L Zetta, H L Monaco.   

Abstract

Bovine beta-LG (beta-lactoglobulin) has been studied under a variety of solution conditions by one- and two-dimensional NMR spectroscopy. At highly acidic pH (pH=2) and low ionic strength the protein is present in a monomeric form, exhibiting a highly structured beta-sheet core and less ordered regions as evidenced by both CD data and the NOESY spectra. Marginal protection was observed for most of the amide protons as a result of high conformational mobility. This structural state of beta-LG may be considered as an attractive model for a partially folded structure occurring late in the folding process of the protein.

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Year:  1996        PMID： 8601463     DOI： 10.1016/0014-5793(96)00100-7

Source DB:  PubMed          Journal:  FEBS Lett        ISSN： 0014-5793            Impact factor:   4.124


  12 in total

1.  New insight into the pH-dependent conformational changes in bovine beta-lactoglobulin from Raman optical activity.

Authors:  E W Blanch; L Hecht; L D Barron
Journal:  Protein Sci       Date:  1999-06       Impact factor: 6.725

2.  Resolution of ligand positions by site-directed tryptophan fluorescence in tear lipocalin.

Authors:  O K Gasymov; A R Abduragimov; T N Yusifov; B J Glasgow
Journal:  Protein Sci       Date:  2000-02       Impact factor: 6.725

3.  Environmentally induced reversible conformational switching in the yeast cell adhesion protein alpha-agglutinin.

Authors:  H Zhao; M H Chen; Z M Shen; P C Kahn; P N Lipke
Journal:  Protein Sci       Date:  2001-06       Impact factor: 6.725

4.  Bovine beta-lactoglobulin: interaction studies with palmitic acid.

Authors:  L Ragona; F Fogolari; L Zetta; D M Pérez; P Puyol; K De Kruif; F Löhr; H Rüterjans; H Molinari
Journal:  Protein Sci       Date:  2000-07       Impact factor: 6.725

5.  Structural changes of beta-lactoglobulin during thermal unfolding and refolding--an FT-IR and circular dichroism study.

Authors:  C Bhattacharjee; S Saha; A Biswas; M Kundu; L Ghosh; K P Das
Journal:  Protein J       Date:  2005-01       Impact factor: 2.371

6.  Glucosylation of beta-lactoglobulin lowers the heat capacity change of unfolding; a unique way to affect protein thermodynamics.

Authors:  Annemarie M M van Teeffelen; Kerensa Broersen; Harmen H J de Jongh
Journal:  Protein Sci       Date:  2005-06-29       Impact factor: 6.725

7.  Effect of temperature on the secondary structure of beta-lactoglobulin at pH 6.7, as determined by CD and IR spectroscopy: a test of the molten globule hypothesis.

Authors:  X L Qi; C Holt; D McNulty; D T Clarke; S Brownlow; G R Jones
Journal:  Biochem J       Date:  1997-05-15       Impact factor: 3.857

8.  Bovine β-lactoglobulin is dimeric under imitative physiological conditions: dissociation equilibrium and rate constants over the pH range of 2.5-7.5.

Authors:  Davide Mercadante; Laurence D Melton; Gillian E Norris; Trevor S Loo; Martin A K Williams; Renwick C J Dobson; Geoffrey B Jameson
Journal:  Biophys J       Date:  2012-07-17       Impact factor: 4.033

9.  Endonuclease activity in lipocalins.

Authors:  T N Yusifov; A R Abduragimov; O K Gasymov; B J Glasgow
Journal:  Biochem J       Date:  2000-05-01       Impact factor: 3.857

10.  Complete assignment of 1H, 13C and 15N chemical shifts for bovine beta-lactoglobulin: secondary structure and topology of the native state is retained in a partially unfolded form.

Authors:  S Uhrínová; D Uhrín; H Denton; M Smith; L Sawyer; P N Barlow
Journal:  J Biomol NMR       Date:  1998-07       Impact factor: 2.835
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