Effects of Polar Head Nature and Tail Length of Single-Chain Lipids on the Conformational Stability of β-Lactoglobulin-Reference-Cited by-同舟云学术

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Effects of Polar Head Nature and Tail Length of Single-Chain Lipids on the Conformational Stability of β-Lactoglobulin

Published:2020-01-22 Issue:6 Volume:124 Page:944-952
ISSN:1520-6106
Container-title:The Journal of Physical Chemistry B
language:en
Short-container-title:J. Phys. Chem. B

Author:

Rizzuti Bruno¹^ORCID,Bartucci Rosa²^ORCID,Guzzi Rita¹³^ORCID

Affiliation:

1. CNR-NANOTEC, Licryl-UOS Cosenza and CEMIF.Cal, Department of Physics, University of Calabria, 87036 Rende, Italy

2. Department of Chemistry and Chemical Technologies and Molecular Biophysics Laboratory, University of Calabria, 87036 Rende, Italy

3. Department of Physics, Molecular Biophysics Laboratory, University of Calabria, 87036 Rende, Italy

Publisher

American Chemical Society (ACS)

Subject

Materials Chemistry,Surfaces, Coatings and Films,Physical and Theoretical Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.jpcb.9b09925

Reference45 articles.

1. Invited Review: β-Lactoglobulin: Binding Properties, Structure, and Function

2. Characterization of pH-induced transitions of β-lactoglobulin: ultrasonic, densimetric, and spectroscopic studies 1 1Edited by C. R. Matthews

3. Systematic calorimetric studies of proton exchange associated with binding of beta-lactoglobulin with ligand

4. Catalytic activity of copper ions in the amyloid fibrillation of β-lactoglobulin

5. Native β-Lactoglobulin Self-Assembles into a Hexagonal Columnar Phase on a Solid Surface

Cited by 2 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Characterization of the interaction of metal-protoporphyrins photosensitizers with β- lactoglobulin;Biophysical Chemistry;2023-01

2. Effect of the hydrophobic phase on interfacial phenomena of surfactants, proteins, and particles at fluid interfaces;Current Opinion in Colloid & Interface Science;2021-12

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