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The role of hydrophobic interactions in the molten globule state of globular protein modulated by surfactants.
Colloids Surf B Biointerfaces
October 2023
Instituto de Física, Universidade de São Paulo, São Paulo, Brazil. Electronic address:
In order to highlight the role of hydrophobic interactions in the molten globule (MG) state of globular protein modulated by surfactants, the interactions of bovine α-lactalbumin (α-LA) with alkyl trimethylammonium bromides (CTAB, n = 10, 12, 14, and 16) have been studied by experimental and theoretical techniques. Isothermal titration calorimetry (ITC) showed that the enthalpy changes (ΔH) and area of the enthalpogram increased with increasing the chain length of CTAB. The result of fluorescence, circular dichroism (CD) and H nuclear magnetic resonance (NMR) spectrum suggested that C10TAB and C12TAB unfolded α-LA partially, C14TAB reconstructed protein with a native-like secondary structure content, and C16TAB induced an MG state α-LA.
View Article and Find Full Text PDFZinc binding strength of proteins dominants zinc uptake in Caco-2 cells.
RSC Adv
July 2022
College of Food Science and Nutritional Engineering, Key Laboratory of Precision Nutrition and Food Quality, Ministry of Education, China Agricultural University Beijing 100083 China
Zinc plays a vital role in structural, catalysis, and signal regulation in the human body. Zinc deficiency leads to the dysfunction of many organs and immunity systems. Diet proteins have distinct effects on zinc uptake.
View Article and Find Full Text PDFUnfolding bovine α-lactalbumin with T-jump: Characterizing disordered intermediates via time-resolved x-ray solution scattering and molecular dynamics simulations.
J Chem Phys
March 2021
Department of Chemistry, Northwestern University, Evanston, Illinois 60208, USA.
The protein folding process often proceeds through partially folded transient states. Therefore, a structural understanding of these disordered states is crucial for developing mechanistic models of the folding process. Characterization of unfolded states remains challenging due to their disordered nature, and incorporating multiple methods is necessary.
View Article and Find Full Text PDFThe influence of pH, protein concentration and calcium ratio on the formation and structure of nanotubes from partially hydrolyzed bovine α-lactalbumin.
Soft Matter
June 2019
Section for Ingredients and Dairy Technology, Department of Food Science, University of Copenhagen, Rolighedsvej 30, DK-1958 Frederiksberg C, Denmark.
Formation of nanotubes from partially hydrolysed α-lactalbumin (α-La) was investigated at five pH values, two concentrations of α-La and two calcium levels. Nanotubes were formed under almost all combinations of the investigated factors, and for the first time the formation of nanotubes at low pH (4.0) and low protein concentration (10 g l-1) was observed.
View Article and Find Full Text PDFEffect of nonenzymatic deamidation on the structure stability of Camelus dromedarius α-lactalbumin.
Food Chem
September 2019
Université de Lorraine, INRA, Unité de Recherche Animal et Fonctionnalités des Produits Animaux (UR AFPA), USC 340, Nancy F-54000, France. Electronic address:
Camelid α-lactalbumin is the only known protein that can undergo nonenzymatic deamidation on two Asn residues. This leads to the generation of a mixture of unusual isoAsp and d-Asp residues that may impact health. The effect of deamidation on camel α-lactalbumin instability was investigated.
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