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Salannal

$954

  • Brand : BIOFRON

  • Catalogue Number : BN-O1510

  • Specification : 98%(HPLC)

  • CAS number : 86160-86-3

  • Formula : C34H44O10

  • Molecular Weight : 612.7

  • PUBCHEM ID : 15226770

  • Volume : 5mg

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Catalogue Number

BN-O1510

Analysis Method

Specification

98%(HPLC)

Storage

2-8°C

Molecular Weight

612.7

Appearance

Botanical Source

Structure Type

Category

SMILES

CC=C(C)C(=O)OC1CC(C(C2C1(C(C3(C(C2OC(=O)C)OC4C3=C(C(C4)C5=COC=C5)C)C)CC(=O)OC)C)(C)C=O)O

Synonyms

IUPAC Name

[(1S,2R,3R,4S,5R,7S,8R,9R,10R,13R,15R)-2-acetyloxy-4-formyl-13-(furan-3-yl)-5-hydroxy-9-(2-methoxy-2-oxoethyl)-4,8,10,12-tetramethyl-16-oxatetracyclo[8.6.0.03,8.011,15]hexadec-11-en-7-yl] (E)-2-methylbut-2-enoate

Density

Solubility

Flash Point

Boiling Point

Melting Point

InChl

InChl Key

JOVDKZRXWAATEG-REXVOHEDSA-N

WGK Germany

RID/ADR

HS Code Reference

Personal Projective Equipment

Correct Usage

For Reference Standard and R&D, Not for Human Use Directly.

Meta Tag

provides coniferyl ferulate(CAS#:86160-86-3) MSDS, density, melting point, boiling point, structure, formula, molecular weight etc. Articles of coniferyl ferulate are included as well.>> amp version: coniferyl ferulate

No Technical Documents Available For This Product.

PMID

27641490

Abstract

Membrane proteins employ specific distribution patterns of amino acids in their tertiary structure for adaptation to their unique bilayer environment. The solvent-bilayer interface, in particular, displays the characteristic ‘aromatic belt’ that defines the transmembrane region of the protein, and satisfies the amphipathic interfacial environment. Tryptophan—the key residue of this aromatic belt—is known to influence the folding efficiency and stability of a large number of well-studied α-helical and β-barrel membrane proteins. Here, we have used functional and biophysical techniques coupled with simulations, to decipher the contribution of strategically placed four intrinsic tryptophans of the human outer mitochondrial membrane protein, voltage-dependent anion channel isoform-2 (VDAC-2). We show that tryptophans help in maintaining the structural and functional integrity of folded hVDAC-2 barrel in micellar environments. The voltage gating characteristics of hVDAC-2 are affected upon mutation of tryptophans at positions 75, 86 and 221. We observe that Trp-160 and Trp-221 play a crucial role in the folding pathway of the barrel, and once folded, Trp-221 helps stabilize the folded protein in concert with Trp-75 and Trp-160. We further demonstrate that substituting Trp-86 with phenylalanine leads to the formation of stable barrel. We find that the region comprising strand β4 (Trp-86) and β10-14 (Trp-160 and Trp-221) display slower and faster folding kinetics, respectively, providing insight into a possible directional folding of hVDAC-2 from the C-terminus to N-terminus. Our results show that residue selection in a protein during evolution is a balancing compromise between optimum stability, function, and regulating protein turnover inside the cell.

Abbreviations: ΔG0, apparent Gibbs free energy of unfolding/folding derived from equilibrium chemical denaturation, ΔG0kin, apparent Gibbs free energy of unfolding/folding obtained from folding/unfolding kinetic (chevron plots), ΔHapp, apparent unfolding cooperativity in thermal denaturation, <τ>, tryptophan lifetime, CD, circular dichroism, Cm, chemical denaturation mid-point, DDM, dodecyl β-d-maltoside, DiPhPC, diphytanoylphosphatidyl choline, GdnHCl, guanidine hydrochloride, hVDAC-2, human voltage dependent anion channel isoform-2, KSV, Stern-Volmer quenching constant, m, apparent unfolding/folding cooperativity, ME214-216, average of molar ellipticity values between 214-216 nm, OMM, outer mitochondrial membrane, Rg, radius of gyration, RMSD, root mean square deviation, RMSF, root mean square fluctuation, SAS, solvent accessible surface, Tm, mid-point of thermal denaturation, Tm-start, start temperature of thermal denaturation, WT, wild-type hVDAC-2 protein

KEYWORDS

VDAC-2, Tryptophans, Stability, Thermodynamics, Kinetics

Title

Control of human VDAC-2 scaffold dynamics by interfacial tryptophans is position specific

Author

Svetlana Rajkumar Maurya and Radhakrishnan Mahalakshmi⁎

Publish date

2016 Dec;

PMID

27509503

Abstract

The Beidou navigation satellite system is a very important sensor for positioning in the Asia-Pacific region. The Beidou inclined geosynchronous orbit (IGSO) and medium Earth orbit (MEO) satellites have been analysed in some studies previously conducted by other researchers; this paper seeks to gain more insight regarding the geostationary earth orbit (GEO) satellites. Employing correlation analysis, Fourier transformation and wavelet decomposition, we validate whether there is a systematic bias in their multipath combinations. These biases can be observed clearly in satellites C01, C02 and C04 and have a great correlation with time series instead of elevation, being significantly different from those of the Beidou IGSO and MEO satellites. We propose a correction model to mitigate this bias based on its daily periodicity characteristic. After the model has been applied, the performance of the positioning estimations of the eight stations distributed in the Asia-Pacific region is evaluated and compared. The results show that residuals of multipath series behaves random noise; for the single point positioning (SPP) and precise point positioning (PPP) approaches, the positioning accuracy in the upward direction can be improved by 8 cm and 6 mm, respectively, and by 2 cm and 4 mm, respectively, for the horizontal component.

KEYWORDS

Beidou GEO, multipath combinations, code bias, correction model

Title

Analysis of the Bias on the Beidou GEO Multipath Combinations

Author

Yafei Ning,1,2,* Yunbin Yuan,1 Yanju Chai,1 and Yong Huang3

Publish date

2016 Aug;

PMID

31139393

Abstract

The present investigation aimed at evaluating the effect of powder fractionation based on particle size on the chemical composition in macronutrients, polyphenol contents, and antioxidant properties of powders of Boscia senegalensis seeds, Dichrostachys glomerata fruits, and Hibiscus sabdariffa calyces. Significant differences (p < 0.05) among granulometric classes of each plant were observed for the chemical composition in macronutrients. A decrease in particle size of plant powders was associated with an increase in ash, protein, and fat contents, while carbohydrate content was lowered. The following Granulometric classes, [0-180 µm] for Boscia senegalensis, [180-212 µm] for Dichrostachys glomerata, and [212-315 µm] for Hibiscus sabdariffa, respectively, were found to maximize total phenolic content and antioxidant activity. These results confirm that the grinding and controlled differential screening technology is an approach may serve as a useful guide to obtain optimum polyphenol extraction and enhance antioxidant activity of plant products.

KEYWORDS

antioxidant activity, chemical composition, particle size, plant powders, polyphenols, sieving

Title

Successive grinding and sieving as a new tool to fractionate polyphenols and antioxidants of plants powders: Application to Boscia senegalensis seeds, Dichrostachys glomerata fruits, and Hibiscus sabdariffa calyx powders

Author

Markusse Deli, 1 Elie Baudelaire Ndjantou, 1 Josiane Therese Ngatchic Metsagang, 1 Jeremy Petit, 2 Nicolas Njintang Yanou,corresponding author 3 and Joël Scher 2

Publish date

2019 May;


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