Journal ArticleDOI
Interaction of milk α- and β-caseins with tea polyphenols
TLDR
In this article, the polyphenol binding mode, the binding constant and the effects of polyphenolic complexation on casein stability and conformation were determined using FTIR, UV-visible, CD and fluorescence spectroscopic methods as well as molecular modelling.About:
This article is published in Food Chemistry.The article was published on 2011-05-15. It has received 328 citations till now. The article focuses on the topics: Casein & Polyphenol.read more
Citations
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Journal ArticleDOI
A review on protein–phenolic interactions and associated changes
TL;DR: In this article, the effects of protein-phenolic interactions under various conditions on protein and phenolic compound's structure and functionality are described, including temperature, pH, protein type and concentration, and the type and structure of phenolic compounds.
Journal ArticleDOI
Interactions of polyphenols with carbohydrates, lipids and proteins
TL;DR: The interactions between phenolic compounds and lipids, carbohydrates and proteins and their impact on polyphenol activity are reviewed.
Journal ArticleDOI
Milk β-lactoglobulin complexes with tea polyphenols.
C.D. Kanakis,Imed Hasni,P. Bourassa,Petros A. Tarantilis,Moschos G. Polissiou,H.A. Tajmir-Riahi +5 more
TL;DR: The β-LG conformation was altered in the presence of polyphenols with an increase in β-sheet and α-helix suggesting protein structural stabilisation, which can be used to explain the mechanism by which the antioxidant activity of tea compounds is affected by the addition of milk.
Journal ArticleDOI
Protein–polyphenol conjugates: Antioxidant property, functionalities and their applications
TL;DR: The protein-polyphenol conjugates with higher thermal stability, antioxidant activities, better emulsifying properties and enhanced gelling property can be used as novel food additives for improvement of functionalities and quality of food products.
Journal ArticleDOI
Recent developments on polyphenol–protein interactions: effects on tea and coffee taste, antioxidant properties and the digestive system
TL;DR: This review summarizes the recent trends and patterns (2005 onwards) in polyphenol-protein interaction studies focusing on the characterization of the complex, the effect of this complex formation on tea and coffee taste, antioxidant properties and the digestive system.
References
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Journal ArticleDOI
Estimation of Protein Secondary Structure from Circular Dichroism Spectra: Comparison of CONTIN, SELCON, and CDSSTR Methods with an Expanded Reference Set
TL;DR: Analyzing protein CD spectra using all three methods should improve the reliability of predicted secondary structural fractions, and three programs are provided in CDPro software package and have been modified for easier use with the different reference sets described in this paper.
Journal ArticleDOI
Examination of the secondary structure of proteins by deconvolved FTIR spectra.
D M Byler,H. Susi +1 more
TL;DR: Fourier transform ir (FTIR) spectra of 21 globular proteins have been obtained, revealing that the amide I band of each protein except casein consists of six to nine components, although all proteins do not exhibit components at every characteristic frequency.
Book ChapterDOI
Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins.
Samuel Krimm,Jagdeesh Bandekar +1 more
TL;DR: The aim of this chapter is to present recent developments in the vibrational spectroscopy of peptides, polypeptides, and proteins.
Journal ArticleDOI
Natively unfolded proteins: a point where biology waits for physics.
TL;DR: Results of this analysis showed that intrinsically unstructured proteins do not possess uniform structural properties, as expected for members of a single thermodynamic entity, and the Protein Quartet model, with function arising from four specific conformations (ordered forms, molten globule, premolten globules, and random coils) is discussed.
Book
Binding Constants: The Measurement of Molecular Complex Stability
TL;DR: This paper presents a method for quantifying theSolubility of Binding Constants using Optical Absorption Spectroscopy and Magnetic Resonance spectroscopy, and its applications in medicine and materials science.