Methyl 2-(4-chloro-3,5-dinitrobenzamido)acetate

Wu, Xiangxiang; Wu, Xia; Hou, Yimin; Ng, Seik Weng; Tiekink, Edward R. T.

doi:10.1107/s1600536811050446

Cited by 2 publications

(2 citation statements)

References 6 publications

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“…Glycylglycylglycine was purchased from Alfa Aeasar and used as received (99%, Ward Hill, MA). The synthesis of N -acetyltriglycinamide was performed by starting from an N -acetyldiglycine precursor. , Specifically, diglycine was modified by acetylation of its N-terminus, followed by conjugation with glycinamide. The NaSCN, NaI, NaBr, and Na 2 SO 4 employed in the NMR experiments was purchased from Sigma Aldrich (St. Louis,MO), while NaCl came from VWR (Radnor, PA).…”

Section: Methodsmentioning

confidence: 99%

Reversal of the Hofmeister Series: Specific Ion Effects on Peptides

et al. 2013

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Ion-specific effects on salting-in and salting-out of proteins, protein denaturation, as well as enzymatic activity are typically rationalized in terms of the Hofmeister series. Here, we demonstrate by means of NMR spectroscopy and molecular dynamics simulations that the traditional explanation of the Hofmeister ordering of ions in terms of their bulk hydration properties is inadequate. Using triglycine as a model system, we show that the Hofmeister series for anions changes from a direct to a reversed series upon uncapping the N-terminus. Weakly hydrated anions, such as iodide and thiocyanate, interact with the peptide bond, while strongly hydrated anions like sulfate are repelled from it. In contrast, reversed order in interactions of anions is observed at the positively charged, uncapped N-terminus, and by analogy, this should also be the case at side chains of positively charged amino acids. These results demonstrate that the specific chemical and physical properties of peptides and proteins play a fundamental role in ion-specific effects. The present study thus provides a molecular rationalization of Hofmeister ordering for the anions. It also provides a route for tuning these interactions by titration or mutation of basic amino acid residues on the protein surface.

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Section: Methodsmentioning

confidence: 99%

Reversal of the Hofmeister Series: Specific Ion Effects on Peptides

et al. 2013

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“…For the biological activity of compounds with nitro and ester groups, see: Sykes et al (1999). For a related structure, see: Wu et al (2011).…”

Section: Related Literaturementioning

confidence: 99%

Methyl 2-(4-methoxy-3-nitrobenzamido)acetate

Zhu

2012

Acta Cryst E

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The title compound, C11H12N2O6, crystallizes with two independent molecules in the asymmetric unit, which differ slightly in conformation. The dihedral angle between the amide O=C—N plane and the attached benzene ring is 19.5 (3)° in one molecule and 23.4 (3)° in the other. In the crystal, the two independent molecules are connected alternately by N—H⋯O hydrogen bonds, forming a chain along the a axis.

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Methyl 2-(4-chloro-3,5-dinitrobenzamido)acetate

Cited by 2 publications

References 6 publications

Reversal of the Hofmeister Series: Specific Ion Effects on Peptides

Reversal of the Hofmeister Series: Specific Ion Effects on Peptides

Methyl 2-(4-methoxy-3-nitrobenzamido)acetate

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