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Merck
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重要文件

215260

Sigma-Aldrich

氯化铷

99.8% trace metals basis

同義詞:

Rubidium monochloride, Rubidium(I) chloride

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About This Item

線性公式:
RbCl
CAS號碼:
分子量::
120.92
EC號碼:
MDL號碼:
分類程式碼代碼:
12352302
PubChem物質ID:
NACRES:
NA.23
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等級

for analytical purposes

化驗

99.8% trace metals basis

形狀

powder and chunks

雜質

≤2500.0 ppm Trace Rare Earth Analysis

mp

715 °C (lit.)

密度

2.8 g/mL at 25 °C (lit.)

SMILES 字串

[Cl-].[Rb+]

InChI

1S/ClH.Rb/h1H;/q;+1/p-1

InChI 密鑰

FGDZQCVHDSGLHJ-UHFFFAOYSA-M

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應用

RbCl 是一种碱卤化物,可用于掺杂 L-丙氨酸氯化氢一水合物单晶以改变其介电属性。[1]

儲存類別代碼

11 - Combustible Solids

水污染物質分類(WGK)

WGK 2

閃點(°F)

Not applicable

閃點(°C)

Not applicable

個人防護裝備

Eyeshields, Gloves, type N95 (US)


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Growth, structural, spectral, mechanical and dielectric characterization of RbCl-doped l-alanine hydrogen chloride monohydrate single crystals
Rose AL, et al.
Physica B: Condensed Matter, 406.3, 412-417 (2011)
M L Główka et al.
Acta crystallographica. Section D, Biological crystallography, 61(Pt 4), 433-441 (2005-04-05)
Gramicidin D (gD) is a naturally occurring ionophoric antibiotic that forms membrane channels specific for monovalent cations. The crystal structure of the RbCl complex of gD has been determined at 1.14 A resolution from low-temperature (100 K) synchrotron-radiation data with
Ferenc Horkay et al.
The Journal of chemical physics, 125(23), 234904-234904 (2006-12-28)
The distribution of counterions in solutions of high molecular mass hyaluronic acid, in near-physiological conditions where mono- and divalent ions are simultaneously present, is studied by small angle neutron scattering and anomalous small angle x-ray scattering. The solutions contain either
Amer Alam et al.
Nature structural & molecular biology, 16(1), 30-34 (2008-12-23)
We report the crystal structure of the nonselective cation channel NaK from Bacillus cereus at a resolution of 1.6 A. The structure reveals the intracellular gate in an open state, as opposed to the closed form reported previously, making NaK
Balasundaresan Dhakshnamoorthy et al.
Journal of molecular biology, 396(2), 293-300 (2009-11-26)
The OmpF porin from the Escherichia coli outer membrane folds into a trimer of beta-barrels, each forming a wide aqueous pore allowing the passage of ions and small solutes. A long loop (L3) carrying multiple acidic residues folds into the

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