Pigment−Pigment and Pigment−Protein Interactions in Recombinant Water-Soluble Chlorophyll Proteins (WSCP) from Cauliflower

2007 ◽  
Vol 111 (46) ◽  
pp. 13325-13335 ◽  
Author(s):  
C. Theiss ◽  
I. Trostmann ◽  
S. Andree ◽  
F. J. Schmitt ◽  
T. Renger ◽  
...  
Keyword(s):  
Protein Interactions ◽  
Water Soluble

scholarly journals New Di- and Triorganotin(IV) Tyrosylalaninates as Models for Metal—Protein Interactions: Synthesis, Structural Characterization, and Potentiometric Studies of Tyrosylalanine, Glycyltyrosine, and Glycylisoleucine with Di- and Trimethyltin(IV) Moieties in Aqueous Medium

2012 ◽  
Vol 2012 ◽  
pp. 1-13 ◽  
Author(s):  
Mala Nath ◽  
Sulaxna ◽  
Xueqing Song ◽  
George Eng
Keyword(s):  
Protein Interactions ◽  
Water Soluble ◽  
Tridentate Ligand ◽  
Spectroscopic Techniques ◽  
Complex Species ◽  
Carboxylate Oxygen ◽  
Trigonal Bipyramidal ◽  
Bipyramidal Structure ◽  
Ft Ir ◽  
Ph Range

Di- and triorganotin(IV) derivatives of tyrosylalanine (H2Tyr-Ala) with general formula R2Sn(Tyr-Ala) (where R = Me, n-Bu, n-Oct, and Ph) and R3Sn(HTyr-Ala) (where R = Me and Ph) have been synthesized and structurally characterized in the solid state as well as in solution on the basis of various spectroscopic techniques, namely. FT-IR, multinuclear (1H, 13C and 119Sn) NMR and 119Sn Mössbauer. These investigations suggest that tyrosylalanine in R2Sn(Tyr-Ala) acts as dianionic tridentate ligand coordinating through carboxylate oxygen [–C(O)O−], amino (–NH2), and (CO)Npeptide- nitrogen, while in the case of R3Sn(HTyr-Ala), the ligand acts as monoanionic bidentate coordinating through –C(O)O− and –NH2, and the polyhedron around tin in R2Sn(Tyr-Ala) and R3Sn(HTyr-Ala) is a distorted trigonal-bipyramidal. Equilibrium (pH-metric) studies of the interaction of Me2Sn(IV)2+ and Me3Sn(IV)+ with dipeptides namely, tyrosylalanine (H2Tyr-Ala), glycyltyrosine (H2Gly-Tyr), and glycylisoleucine (H2Gly-Ile), in aqueous solution (I = 0.1 M KNO3, 298 K) have also been carried out. The concentration distribution of the various complex species in solution has been evaluated as a function of pH. It has been found that in these dipeptides, [–C(O)O−, N−, NH2] coordinated complexes are dominant in the neutral pH range with a trigonal-bipyramidal structure. The complex species formed are water soluble in the pH range 2.7–10.5. In all of the studied systems, no polymeric species have been detected in the experimental pH range. Beyond pH 8.0, significant amounts of hydroxo species, namely. Me3Sn(OH) and Me2Sn(OH)2, are formed.

New Water‐Soluble N‐Heterocyclic Carbene‐Palladium Complexes as Promising Anti‐Tumor Agents: Investigating DNA and Protein Interactions

2018 ◽  
Vol 3 (21) ◽  
pp. 5709-5716 ◽  
Author(s):  
Prachi S. Bangde ◽  
Dharmendra S. Prajapati ◽  
Prajakta P. Dandekar ◽  
Anant R. Kapdi
Keyword(s):  
Protein Interactions ◽  
Palladium Complexes ◽  
Water Soluble

scholarly journals Design of Stable α-Helical Peptides and Thermostable Proteins in Biotechnology and Biomedicine

Acta Naturae ◽  
2016 ◽  
Vol 8 (4) ◽  
pp. 70-81 ◽  
Author(s):  
A. P. Yakimov ◽  
A. S. Afanaseva ◽  
M. A. Khodorkovskiy ◽  
M. G Petukhov
Keyword(s):  
Protein Interactions ◽  
Thermophilic Bacteria ◽  
Conformational Stability ◽  
Globular Proteins ◽  
High Thermal Stability ◽  
Water Soluble ◽  
Helical Peptides ◽  
Highly Active ◽  
Thermal Stability Of ◽  
Specific Inhibitors

-Heliсes are the most frequently occurring elements of the secondary structure in water-soluble globular proteins. Their increased conformational stability is among the main reasons for the high thermal stability of proteins in thermophilic bacteria. In addition, -helices are often involved in protein interactions with other proteins, nucleic acids, and the lipids of cell membranes. That is why the highly stable -helical peptides used as highly active and specific inhibitors of protein-protein and other interactions have recently found more applications in medicine. Several different approaches have been developed in recent years to improve the conformational stability of -helical peptides and thermostable proteins, which will be discussed in this review. We also discuss the methods for improving the permeability of peptides and proteins across cellular membranes and their resistance to intracellular protease activity. Special attention is given to the SEQOPT method (http://mml.spbstu.ru/services/seqopt/), which is used to design conformationally stable short -helices.

Synthesis of hyperbranched glycodendrimers incorporating α-thiosialosides based on a gallic acid core

1997 ◽  
Vol 75 (11) ◽  
pp. 1472-1482 ◽  
Author(s):  
Serge J. Meunier ◽  
Quigquan Wu ◽  
Sho-Nong Wang ◽  
René Roy
Keyword(s):  
Sialic Acid ◽  
Gallic Acid ◽  
Protein Interactions ◽  
Wheat Germ Agglutinin ◽  
Wheat Germ ◽  
Water Soluble ◽  
Cross Link ◽  
Binding Studies ◽  
Turbidimetric Analysis ◽  
Dendritic Precursors

Hyperbranched glycodendrimers containing sialic acid residues were synthesized in order to further understand the multivalency effect and its role in carbohydrate–protein interactions. Gallic acid 7 as trivalent core and oligoethylene glycol derivatives as hydrophilic spacers were used to scaffold the dendritic backbones. α-Thiosialoside 16 was conjugated onto N-chloroacetylated dendritic precursors 13,14, and 26 by nucleophilic substitution to afford trivalent 17,18, and nonavalent 27 sialodendrimers. Complete sugar deprotection furnished water-soluble α-thiosialodendrimers 21,22, and 29, which were used in protein-binding studies. Turbidimetric analysis confirmed the strong potential of sialodendrimers 29 having nine readily accessible sialic acid residues to bind, cross-link, and precipitate two different lectins. Preliminary results indicated that nonavalent α-sialodendrimer 29 had a greater affinity towards dimeric wheat germ agglutinin (WGA) and the lectin from the slug Limaxflavus (LFA) than the corresponding trivalent glycodendrimers 21 and 22. Keywords: carbohydrate, dendrimer, sialic acid, gallic acid, lectin, wheat germ agglutinin, Limaxflavus.

scholarly journals Green self-immolative polymer: molecular antenna to collect and propagate the signal for zymogen activation

2021 ◽  
Author(s):  
Mireia Casanovas Montasell ◽  
Pere Monge ◽  
Sheiliza Carmali ◽  
Livia Mesquita ◽  
Dante Andersen ◽  
...  
Keyword(s):  
Protein Interactions ◽  
Water Soluble ◽  
Protein Protein Interactions ◽  
Zymogen Activation ◽  
Protein Thiol ◽  
Disulfide Linkage ◽  
Enzyme Active Site ◽  
Naturally Occurring ◽  
Different Types ◽  
A Chain

Chemical zymogens of three different types were established herein around protein cysteinome, in each case converting the protein thiol into a disulfide linkage: zero length Z0, polyethylene glycol based ZPEG, and ZLA that features a fast-depolymerizing fuse polymer. The latter was a polydisulfide based on a naturally occurring water-soluble lipoic acid. Three zymogen designs were applied to cysteinyl proteases and a kinase and in each case, enzymatic activity was successfully masked in full and reactivated by small molecule reducing agents. However, only ZLA could be reactivated by protein activators, demonstrating that the macromolecular fuse escapes the steric bulk created by the protein globule, collects activation signal in solution, and relays it to the enzyme active site. This afforded first-in-class chemical zymogens that are activated via protein-protein interactions. For ZLA, we also document a "chain transfer" bioconjugation mechanism and a unique zymogen exchange reaction between two proteins.

scholarly journals Effect of Pulsed Electric Fields on the Main Chemical Components of Liquid Egg and Stability at 4°C

2009 ◽  
Vol 27 (Special Issue 1) ◽  
pp. S109-S112 ◽  
Author(s):  
R. Marco-Molés ◽  
I. Pérez-Munuera ◽  
A. Quiles ◽  
I. Hernando
Keyword(s):  
Electric Fields ◽  
Protein Interactions ◽  
Soluble Protein ◽  
Water Soluble ◽  
Chemical Components ◽  
Protein Protein Interactions ◽  
Water Soluble Protein ◽  
Microbiological Stability ◽  
Egg Components ◽  
Oxidation Parameters

The effect of PEF on the whole liquid egg components, proteins and lipids, and the microstructure were studied and compared with pasteurisation. The effect of the refrigerated storage one week after the treatments was too studied. After all the treatments, only pasteurised samples showed water-soluble protein values significantly lower than the control and PEF treated samples, even after refrigeration. This could be related to the reinforcement of protein-protein interactions generated by the partial denaturalisation of proteins, observed by Cryo-SEM. Moreover, a water-soluble protein decrease was detected in the control and PEF treated samples after refrigeration, probably due to the aggregation of the egg lipoprotein during the storage. Furthermore, a slight lipolysis was observed in the control and PEF treated samples after refrigeration; but this effect was lower as higher was the PEF treatment. The study of the oxidation parameters showed an intermediate degradation of the lipids in treated samples, compared to the pasteurised eggs. These would reflect a higher microbiological stability of the PEF treated samples compared to the non-treated eggs.

Solution properties, electrochemical behavior and protein interactions of water soluble triosmium carbonyl clusters

2004 ◽  
Vol 689 (10) ◽  
pp. 1796-1805 ◽  
Author(s):  
Carlo Nervi ◽  
Roberto Gobetto ◽  
Luciano Milone ◽  
Alessandra Viale ◽  
Edward Rosenberg ◽  
...  
Keyword(s):  
Protein Interactions ◽  
Electrochemical Behavior ◽  
Water Soluble ◽  
Solution Properties ◽  
Carbonyl Clusters ◽  
Triosmium Carbonyl Clusters

Excitonic Energy Level Structure and Pigment−Protein Interactions in the Recombinant Water-Soluble Chlorophyll Protein. II. Spectral Hole-Burning Experiments

2011 ◽  
Vol 115 (14) ◽  
pp. 4053-4065 ◽  
Author(s):  
J. Pieper ◽  
M. Rätsep ◽  
I. Trostmann ◽  
F.-J. Schmitt ◽  
C. Theiss ◽  
...  
Keyword(s):  
Energy Level ◽  
Protein Interactions ◽  
Level Structure ◽  
Water Soluble ◽  
Hole Burning ◽  
Spectral Hole Burning ◽  
Energy Level Structure ◽  
Spectral Hole ◽  
Chlorophyll Protein ◽  
Excitonic Energy
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