Role of the Polysaccharide Content and Net Charge on the Emulsifying Properties of β-Lactoglobulin−Carboxymethyldextran Conjugates

1996 ◽  
Vol 44 (9) ◽  
pp. 2538-2543 ◽  
Author(s):  
Koichi Nagasawa ◽  
Koki Ohgata ◽  
Koji Takahashi ◽  
Makoto Hattori
Keyword(s):  
Emulsifying Properties ◽  
Net Charge ◽  
Polysaccharide Content ◽  
Β Lactoglobulin

Studies on Water in Barnacle Muscle Fibres II. Role of ions and Organic Solutes in Swelling of Chemically-skinned Fibres

1981 ◽  
Vol 90 (1) ◽  
pp. 43-63
Author(s):  
M. E. CLARK ◽  
J. A. M. HINKE ◽  
M. E. TODD
Keyword(s):  
Water Content ◽  
Fibre Volume ◽  
Tween 20 ◽  
Muscle Fibres ◽  
Skinned Fibres ◽  
Organic Solutes ◽  
Net Charge ◽  
Trimethylamine Oxide ◽  
Organic Solute

Single muscle fibres from the giant barnacle, Balanus nubilis, were chemically skinned (2% Tween 20), then equilibrated for 40 h in salt solutions ranging in ionic strength from 0·025 to 0·6M at pH 7·0. The water content of the fibres and the net charge on the myofilaments increased with increasing salt concentration. Cation accumulation in the fibres was about equal to anion exclusion at all salt concentrations. When an organic solute (trimethylamine oxide, glycine, alanine, serine, proline, or glycerol) in the concentration range from 0·1 to 0·6 M was added to the salt solution, cation accumulation increased and water content decreased. Myofilament architecture was disrupted when the fibres were equilibrated in high salt (> 0·4 M) solutions and preserved when 0·5 M-triethylamine oxide was also added. The results are consistent with the view that organic solutes enhance the association between the fixed charge sites and their counterions. This hypothesis is examined quantitatively using the Oosawa relationship between the volume and the counterion association for cylindrical polyelectrolytes. The results illustrate that organic solutes can influence fibre volume in a way other than through osmo-regulation.

scholarly journals Arginine-enriched mixed-charge domains provide cohesion for nuclear speckle condensation

2019 ◽  
Author(s):  
Jamie A. Greig ◽  
Tu Anh Nguyen ◽  
Michelle Lee ◽  
Alex S. Holehouse ◽  
Ammon E. Posey ◽  
...  
Keyword(s):  
Low Complexity ◽  
Rna Recognition Motif ◽  
Rna Recognition ◽  
Nuclear Speckle ◽  
Net Charge ◽  
Intrinsically Disordered ◽  
Recognition Motif ◽  
Condensate Formation ◽  
Dynamic Material Properties

AbstractLow-complexity protein domains promote the formation of various biomolecular condensates. However, in many cases, the precise sequence features governing condensate formation and identity remain unclear. Here, we investigate the role of intrinsically disordered mixed-charge domains (MCDs) in nuclear speckle condensation. Proteins composed exclusively of arginine/aspartic-acid dipeptide repeats undergo length-dependent condensation and speckle incorporation. Substituting arginine with lysine in synthetic and natural speckle-associated MCDs abolishes these activities, identifying a key role for multivalent contacts through arginine’s guanidinium ion. MCDs can synergise with a speckle-associated RNA recognition motif to promote speckle specificity and residence. MCD behaviour is tuneable through net-charge: increasing negative charge abolishes condensation and speckle incorporation. By contrast, increasing positive charge through arginine leads to enhanced condensation, speckle enlargement, decreased splicing factor mobility, and defective mRNA export. Together, these results identify key sequence determinants of MCD-promoted speckle condensation, and link the speckle’s dynamic material properties with function in mRNA processing.

Role of Pyridoxamine in the Formation of the Amadori/Heyns Compounds and Aggregates during the Glycation of β-Lactoglobulin with Galactose and Tagatose

2010 ◽  
Vol 58 (1) ◽  
pp. 500-506 ◽  
Author(s):  
Marta Corzo-Martínez ◽  
F. Javier Moreno ◽  
Agustín Olano ◽  
Mar Villamiel
Keyword(s):  
Β Lactoglobulin

scholarly journals Exciton-to-trion conversion as a control mechanism for valley polarization in room-temperature monolayer WS2

2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Joris J. Carmiggelt ◽  
Michael Borst ◽  
Toeno van der Sar
Keyword(s):  
Room Temperature ◽  
Polarized Light ◽  
Optical Excitation ◽  
Equation Model ◽  
Chemical Doping ◽  
Transition Metal Dichalcogenide ◽  
Net Charge ◽  
Circularly Polarized Light ◽  
Valley Polarization

Abstract Transition metal dichalcogenide (TMD) monolayers are two-dimensional semiconductors with two valleys in their band structure that can be selectively addressed using circularly polarized light. Their photoluminescence spectrum is characterized by neutral and charged excitons (trions) that form a chemical equilibrium governed by the net charge density. Here, we use chemical doping to drive the conversion of excitons into trions in $$\text {WS}_{2}$$ WS 2 monolayers at room temperature, and study the resulting valley polarization via photoluminescence measurements under valley-selective optical excitation. We show that the doping causes the emission to become dominated by trions with a strong valley polarization associated with rapid non-radiative recombination. Simultaneously, the doping results in strongly quenched but highly valley-polarized exciton emission due to the enhanced conversion into trions. A rate equation model explains the observed valley polarization in terms of the doping-controlled exciton-trion equilibrium. Our results shed light on the important role of exciton-trion conversion on valley polarization in monolayer TMDs.

Effect of high pressure homogenization on the structure and the interfacial and emulsifying properties of β-lactoglobulin

2018 ◽  
Vol 537 (1-2) ◽  
pp. 111-121 ◽  
Author(s):  
Ali Ali ◽  
Isabelle Le Potier ◽  
Nicolas Huang ◽  
Véronique Rosilio ◽  
Monique Cheron ◽  
...  
Keyword(s):  
High Pressure ◽  
High Pressure Homogenization ◽  
Emulsifying Properties ◽  
Β Lactoglobulin

scholarly journals Evidence for β-lactoglobulin involvement in vitamin D transportin vivo- role of the γ-turn (Leu-Pro-Met) of β-lactoglobulin in vitamin D binding

FEBS Journal ◽  
2009 ◽  
Vol 276 (8) ◽  
pp. 2251-2265 ◽  
Author(s):  
Ming Chi Yang ◽  
Nai Chi Chen ◽  
Chun-Jung Chen ◽  
Chin Yun Wu ◽  
Simon J. T. Mao
Keyword(s):  
Vitamin D ◽  
Β Lactoglobulin

scholarly journals β-Lactoglobulin-linoleate complexes: In vitro digestion and the role of protein in fatty acid uptake

2013 ◽  
Vol 96 (7) ◽  
pp. 4258-4268 ◽  
Author(s):  
Solène Le Maux ◽  
André Brodkorb ◽  
Thomas Croguennec ◽  
Alan A. Hennessy ◽  
Saïd Bouhallab ◽  
...  
Keyword(s):  
Fatty Acid ◽  
In Vitro Digestion ◽  
Fatty Acid Uptake ◽  
Acid Uptake ◽  
Β Lactoglobulin

scholarly journals Binding of CML-Modified as Well as Heat-Glycated β-lactoglobulin to Receptors for AGEs Is Determined by Charge and Hydrophobicity

2020 ◽  
Vol 21 (12) ◽  
pp. 4567 ◽  
Author(s):  
Hannah E. Zenker ◽  
Malgorzata Teodorowicz ◽  
Arifa Ewaz ◽  
R.J. Joost van Neerven ◽  
Huub F.J. Savelkoul ◽  
...  
Keyword(s):  
Secondary Structure ◽  
Tertiary Structure ◽  
Glyoxylic Acid ◽  
Native Page ◽  
Galectin 3 ◽  
Carboxymethyl Lysine ◽  
Antigen Presenting ◽  
Age Receptors ◽  
Β Lactoglobulin

Intake of dietary advanced glycation end products (AGEs) is associated with inflammation-related health problems. Nε-carboxymethyl lysine (CML) is one of the best characterised AGEs in processed food. AGEs have been described as ligands for receptors present on antigen presenting cells. However, changes in protein secondary and tertiary structure also induce binding to AGE receptors. We aimed to discriminate the role of different protein modifications in binding to AGE receptors. Therefore, β-lactoglobulin was chemically modified with glyoxylic acid to produce CML and compared to β-lactoglobulin glycated with lactose. Secondary structure was monitored with circular dichroism, while hydrophobicity and formation of β-sheet structures was measured with ANS-assay and ThT-assay, respectively. Aggregation was monitored using native-PAGE. Binding to sRAGE, CD36, and galectin-3 was measured using inhibition ELISA. Even though no changes in secondary structure were observed in all tested samples, binding to AGE receptors increased with CML concentration of CML-modified β-lactoglobulin. The negative charge of CML was a crucial determinant for the binding of protein bound CML, while binding of glycated BLG was determined by increasing hydrophobicity. This shows that sRAGE, galectin-3, and CD36 bind to protein bound CML and points out the role of negatively charged AGEs in binding to AGE receptors.

Role of the interfaces and the charge of a molecule in the non-equilibrium crystallization of dipeptide nanomaterials onto solid substrates

CrystEngComm ◽  
2018 ◽  
Vol 20 (47) ◽  
pp. 7688-7699 ◽  
Author(s):  
Alexander I. Loskutov ◽  
Boris V. Lokshin ◽  
Tatiana A. Gudasheva ◽  
Vadim B. Oshurko ◽  
Nestor Solis Pinargote ◽  
...  
Keyword(s):  
Critical Role ◽  
Structure And Properties ◽  
Net Charge ◽  
Equilibrium Crystallization ◽  
Solid Substrates ◽  
Non Equilibrium

A critical role of the net charge of molecule and nature of interfaces on the structure and properties of crystallized dipeptide layers was established.

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