pH-Dependent Aggregation and Disaggregation of Native β-Lactoglobulin in Low Salt

Yunfeng Yan; Daniel Seeman; Bingqian Zheng; Ebru Kizilay; Yisheng Xu; Paul L. Dubin

doi:10.1021/la400258r

pH-Dependent Aggregation and Disaggregation of Native β-Lactoglobulin in Low Salt

Langmuir ◽

10.1021/la400258r ◽

2013 ◽

Vol 29 (14) ◽

pp. 4584-4593 ◽

Cited By ~ 49

Author(s):

Yunfeng Yan ◽

Daniel Seeman ◽

Bingqian Zheng ◽

Ebru Kizilay ◽

Yisheng Xu ◽

...

Keyword(s):

Low Salt ◽

Aggregation And Disaggregation ◽

Ph Dependent ◽

Β Lactoglobulin

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1P058 Principal component analysis of the pH-dependent conformational transitions of bovine β-lactoglobulin monitored by heteronuclear NMR(Proteins-functions, methodology, and protein enigineering,Oral Presentations)

Seibutsu Butsuri ◽

10.2142/biophys.47.s38_1 ◽

2007 ◽

Vol 47 (supplement) ◽

pp. S38

Author(s):

Kazumasa Sakurai ◽

Yuji Goto

Keyword(s):

Principal Component Analysis ◽

Heteronuclear Nmr ◽

Principal Component ◽

Component Analysis ◽

Conformational Transitions ◽

Ph Dependent ◽

Oral Presentations ◽

Β Lactoglobulin

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A Tryptophan Rotamer Located in a Polar Environment Probes pH-Dependent Conformational Changes in Bovine β-Lactoglobulin A

The Journal of Physical Chemistry B ◽

10.1021/jp065783a ◽

2007 ◽

Vol 111 (10) ◽

pp. 2610-2620 ◽

Cited By ~ 43

Author(s):

Billie J. Harvey ◽

Erin Bell ◽

Lorenzo Brancaleon

Keyword(s):

Conformational Changes ◽

Polar Environment ◽

Ph Dependent ◽

Β Lactoglobulin

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A 200 nanoseconds all-atom simulation of the pH-dependent EF loop transition in bovine β-lactoglobulin. The role of the orientation of the E89 side chain

Journal of Biomolecular Structure and Dynamics ◽

10.1080/07391102.2020.1817785 ◽

2020 ◽

pp. 1-16 ◽

Cited By ~ 1

Author(s):

Kiara Fenner ◽

Arthur Redgate ◽

Lorenzo Brancaleon

Keyword(s):

Side Chain ◽

Ph Dependent ◽

Β Lactoglobulin

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The pH-dependent conformational transition of β-lactoglobulin modulates the binding of protoporphyrin IX

Biochimica et Biophysica Acta (BBA) - General Subjects ◽

10.1016/j.bbagen.2005.09.005 ◽

2006 ◽

Vol 1760 (1) ◽

pp. 38-46 ◽

Cited By ~ 23

Author(s):

Fang Tian ◽

Katrina Johnson ◽

Andrea E. Lesar ◽

Harry Moseley ◽

James Ferguson ◽

...

Keyword(s):

Conformational Transition ◽

Protoporphyrin Ix ◽

Ph Dependent ◽

Β Lactoglobulin

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

Protein Science ◽

10.1110/ps.8.6.1362 ◽

1999 ◽

Vol 8 (6) ◽

pp. 1362-1367 ◽

Cited By ~ 31

Author(s):

Ewan W. Blanch ◽

Lutz Hecht ◽

Laurence D. Barron

Keyword(s):

Optical Activity ◽

Conformational Changes ◽

Raman Optical Activity ◽

Ph Dependent ◽

Β Lactoglobulin ◽

Insight Into

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A novel pH-dependent dimerization motif in β-lactoglobulin from pig (Sus scrofa)

Acta Crystallographica Section D Biological Crystallography ◽

10.1107/s0907444902000616 ◽

2002 ◽

Vol 58 (3) ◽

pp. 480-486 ◽

Cited By ~ 18

Author(s):

Flip J. Hoedemaeker ◽

Ronald W. Visschers ◽

Arno C. Alting ◽

Kees G. de Kruif ◽

Maxim E. Kuil ◽

...

Keyword(s):

Sus Scrofa ◽

Ph Dependent ◽

Β Lactoglobulin

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pH-Dependent complexation between β-lactoglobulin and lycopene: Multi-spectroscopy, molecular docking and dynamic simulation study

Food Chemistry ◽

10.1016/j.foodchem.2021.130230 ◽

2021 ◽

pp. 130230

Author(s):

Ce wang ◽

Lu chen ◽

Yingcong Lu ◽

Jia Liu ◽

Ru Zhao ◽

...

Keyword(s):

Molecular Docking ◽

Dynamic Simulation ◽

Simulation Study ◽

Ph Dependent ◽

Β Lactoglobulin

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2P125 Relationship between pH-dependent conformational and stability changes of bovine β-lactoglobulin studied using NMR spectroscopy(31. Protein folding and misfolding (II),Poster Session,Abstract,Meeting Program of EABS & BSJ 2006)

Seibutsu Butsuri ◽

10.2142/biophys.46.s327_1 ◽

2006 ◽

Vol 46 (supplement2) ◽

pp. S327

Author(s):

Kazumasa Sakurai ◽

Yuji Goto

Keyword(s):

Protein Folding ◽

Nmr Spectroscopy ◽

Poster Session ◽

Meeting Program ◽

Ph Dependent ◽

Β Lactoglobulin

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Ultrasonic pre-treatment modifies the pH-dependent molecular interactions between β-lactoglobulin and dietary phenolics: conformational structures and interfacial properties

Ultrasonics Sonochemistry ◽

10.1016/j.ultsonch.2021.105612 ◽

2021 ◽

pp. 105612

Author(s):

Qiaozhi Zhang ◽

Huatao Li ◽

Congnan Cen ◽

Jie Zhang ◽

Shunyu Wang ◽

...

Keyword(s):

Molecular Interactions ◽

Interfacial Properties ◽

Ph Dependent ◽

Pre Treatment ◽

Β Lactoglobulin

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Ovine β-lactoglobulin at atomic resolution

Acta Crystallographica Section F Structural Biology Communications ◽

10.1107/s2053230x14020950 ◽

2014 ◽

Vol 70 (11) ◽

pp. 1498-1503 ◽

Cited By ~ 4

Author(s):

George Kontopidis ◽

Anna Nordle Gilliver ◽

Lindsay Sawyer

Keyword(s):

Crystal Structure ◽

High Resolution ◽

Milk Protein ◽

Conformational Transition ◽

Low Ph ◽

Ovis Aries ◽

Atomic Resolution ◽

Ph Dependent ◽

Β Lactoglobulin ◽

Triclinic Form

The crystal structure of the triclinic form of the milk protein β-lactoglobulin from sheep (Ovis aries) at 1.1 Å resolution is described together with a comparison of the triclinic structures of the low-pH bovine and high-pH ovine proteins. All three structures are remarkably similar, despite the well known pH-dependent conformational transition described for the bovine and porcine proteins that occurs in solution. The high resolution of the present structure determination has allowed a more accurate description of the protein than has hitherto been possible, but it is still not clear whether flexibility changes in the external loops can compensate for the presence of a significant void in the unliganded interior of the structure.

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