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Merck

A9502

Sigma-Aldrich

Ala-Ala

别名:

L-丙氨酰-L-丙氨酸

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About This Item

线性分子式:
CH3CH(NH2)CONHCH(CH3)CO2H
CAS号:
分子量:
160.17
Beilstein:
1724813
EC號碼:
MDL號碼:
分類程式碼代碼:
12352209
PubChem物質ID:
NACRES:
NA.26

化驗

≥98% (TLC)

品質等級

形狀

powder

顏色

white

mp

280-285 °C (lit.)

SMILES 字串

C[C@H](N)C(=O)N[C@@H](C)C(O)=O

InChI

1S/C6H12N2O3/c1-3(7)5(9)8-4(2)6(10)11/h3-4H,7H2,1-2H3,(H,8,9)(H,10,11)/t3-,4-/m0/s1

InChI 密鑰

DEFJQIDDEAULHB-IMJSIDKUSA-N

基因資訊

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應用

Ala-Ala 已被用作色谱分析的肽样品。

生化/生理作用

L-丙氨酰-L-丙氨酸被用作模型二肽,用于 pH(质子化)对构象的影响等过程的理化研究。

儲存類別代碼

11 - Combustible Solids

水污染物質分類(WGK)

WGK 3

閃點(°F)

Not applicable

閃點(°C)

Not applicable


历史批次信息供参考:

分析证书(COA)

Lot/Batch Number

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Ladislav Benda et al.
The journal of physical chemistry. B, 113(15), 5273-5281 (2009-03-24)
The dependence of the effective chemical shielding anisotropy (effective CSA, Deltasigma(eff)) on the phi and psi peptide backbone torsion angles was calculated in the l-alanyl-l-alanine (LALA) peptide using the DFT method. The effects of backbone conformation, molecular charge including the
Vladimír Sychrovský et al.
The journal of physical chemistry. B, 112(6), 1796-1805 (2008-01-04)
The l-alanyl-l-alanine (AA) molecule behaves differently in acidic, neutral, and basic environments. Because of its molecular flexibility and strong interaction with the aqueous environment, its behavior has to be deduced from the NMR spectra indirectly, using statistical methods and comparison
Jirí Sebek et al.
The journal of physical chemistry. A, 113(27), 7760-7768 (2009-06-17)
Fine effects of the hydration, charge, and conformational structural changes in L-alanyl-L-alanine (Ala-Ala) dipeptide were studied with the aid of Raman and Raman optical activity (ROA) spectra. The spectra were recorded experimentally and analyzed by means of density functional computations.
Determination of theoretical retention times for peptides analyzed by reversed-phase high-performance liquid chromatography.
Dziuba J, et al.
Acta Scientiarum Polonorum. Technologia Alimentaria, 10(2) (2011)
Yohei M Koyama et al.
Physical review. E, Statistical, nonlinear, and soft matter physics, 84(2 Pt 2), 026704-026704 (2011-09-21)
Conformational fluctuations of a protein molecule are important to its function, and it is known that environmental molecules, such as water molecules, ions, and ligand molecules, significantly affect the function by changing the conformational fluctuations. However, it is difficult to

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