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4-(1H-1,2,4-Triazol-1-ylmethyl)aniline

$87

  • Brand : BIOFRON

  • Catalogue Number : BN-O1056

  • Specification : 98%(HPLC)

  • CAS number : 119192-10-8

  • Formula : C9H10N4

  • Molecular Weight : 174.2

  • PUBCHEM ID : 821219

  • Volume : 5mg

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Catalogue Number

BN-O1056

Analysis Method

Specification

98%(HPLC)

Storage

2-8°C

Molecular Weight

174.2

Appearance

Botanical Source

Structure Type

Category

SMILES

C1=CC(=CC=C1CN2C=NC=N2)N

Synonyms

4-(1H-1,2,4-triazol-1-yl-methyl) aniline/4-(1H-1,2,4-Triazol-1-ylmethyl)aniline/4-[1,2,4]Triazol-1-ylmethyl-phenylamine/4-((1H-1,2,4-Triazol-1-yl)methyl)aniline/Benzenamine, 4-(1H-1,2,4-triazol-1-ylmethyl)-/4-(1,2,4-triazol-1-ylmethyl)aniline/1-(4-Aminobenzyl)-1,2,4-triazole

IUPAC Name

4-(1,2,4-triazol-1-ylmethyl)aniline

Density

1.3±0.1 g/cm3

Solubility

Flash Point

197.0±29.3 °C

Boiling Point

402.1±47.0 °C at 760 mmHg

Melting Point

124 °C

InChl

InChI=1S/C21H20O13/c22-5-11-13(27)15(29)17(31)21(32-11)34-19-10(26)4-9(25)12-14(28)16(30)18(33-20(12)19)6-1-2-7(23)8(24)3-6/h1-4,11,13,15,17,21-27,29-31H,5H2/t11-,13-,15+,17-,21+/m1/s1

InChl Key

ZGLQVRIVLWGDNA-UHFFFAOYSA-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#:119192-10-8) 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

31387291

Title

Correction: Nikitin, D., et al. Retroelement—Linked Transcription Factor Binding Patterns Point to Quickly Developing Molecular Pathways in Human Evolution. Cells 2019, 8, 130

Author

Daniil Nikitin,1,2 Andrew Garazha,2,3 Maxim Sorokin,1,4 Dmitry Penzar,5 Victor Tkachev,2 Alexander Markov,6 Nurshat Gaifullin,7 Pieter Borger,8 Alexander Poltorak,9 and Anton Buzdin1,2,4,*

Publish date

2019 Aug

PMID

32041303

Abstract

“How do proteins fold?” Researchers have been studying different aspects of this question for more than 50 years. The most conceptual aspect of the problem is how protein can find the global free energy minimum in a biologically reasonable time, without exhaustive enumeration of all possible conformations, the so-called “Levinthal’s paradox.” Less conceptual but still critical are aspects about factors defining folding times of particular proteins and about perspectives of machine learning for their prediction. We will discuss in this review the key ideas and discoveries leading to the current understanding of folding kinetics, including the solution of Levinthal’s paradox, as well as the current state of the art in the prediction of protein folding times.

KEYWORDS

protein folding, Levinthal’s paradox, “all-or-none” transition, free energy barrier, folding funnel, detailed balance principle

Title

Solution of Levinthal’s Paradox and a Physical Theory of Protein Folding Times

Author

Dmitry N. Ivankov1,* and Alexei V. Finkelstein2,3,4,*

Publish date

2020 Feb;

PMID

30630950

Abstract

The length of linker DNA that separates nucleosomes is highly variable, but its mechanistic role in modulating chromatin structure and functions remains unknown. Here, we established an experimental system using circular arrays of positioned nucleosomes to investigate whether variations in nucleosome linker length could affect nucleosome folding, self-association, and interactions. We conducted EM, DNA topology, native electrophoretic assays, and Mg2+-dependent self-association assays to study intrinsic folding of linear and circular nucleosome arrays with linker DNA length of 36 bp and 41 bp (3.5 turns and 4 turns of DNA double helix, respectively). These experiments revealed that potential artifacts arising from open DNA ends and full DNA relaxation in the linear arrays do not significantly affect overall chromatin compaction and self-association. We observed that the 0.5 DNA helical turn difference between the two DNA linker lengths significantly affects DNA topology and nucleosome interactions. In particular, the 41-bp linkers promoted interactions between any two nucleosome beads separated by one bead as expected for a zigzag fiber, whereas the 36-bp linkers promoted interactions between two nucleosome beads separated by two other beads and also reduced negative superhelicity. Monte Carlo simulations accurately reproduce periodic modulations of chromatin compaction, DNA topology, and internucleosomal interactions with a 10-bp periodicity. We propose that the nucleosome spacing and associated chromatin structure modulations may play an important role in formation of different chromatin epigenetic states, thus suggesting implications for how chromatin accessibility to DNA-binding factors and the RNA transcription machinery is regulated.

KEYWORDS

chromatin structure, DNA topology, nucleosome, histone, computer modeling, electron microscopy (EM), gene regulation, epigenetics, chromatin higher order structure, linker DNA, conformational simulation, epigenetic regulation

Title

Nucleosome spacing periodically modulates nucleosome chain folding and DNA topology in circular nucleosome arrays

Author

Mikhail V. Bass,‡§ Tatiana Nikitina,¶ Davood Norouzi,¶ Victor B. Zhurkin,¶,1 and Sergei A. Grigoryev‡,2

Publish date

2019 Mar 15;


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