Expression and purification of uniformly 15N-labeled amyloid β peptide 1-40 in Escherichia coli

M. Nagata-Uchiyama; M. Yaguchi; Y. Hirano; Tadashi Ueda

doi:10.2174/092986607781483741

Expression and purification of uniformly ¹⁵N-labeled amyloid β peptide 1-40 in Escherichia coli

M. Nagata-Uchiyama, M. Yaguchi, Y. Hirano, Tadashi Ueda

Pharmaceutical Health Care and Sciences

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14 Citations (Scopus)

Abstract

For biophysical studies using heteronuclear NMR analysis of amyloid beta peptide, construction of an efficient and high yield expression system of uniformly isotopic labeled amyloid beta peptide is desirable. Here we succeeded in obtaining ¹⁵N-labeled amyloid beta 1-40 expressed by attachment to hen egg white lysozyme as a fusion protein.

Original language	English
Pages (from-to)	788-792
Number of pages	5
Journal	Protein and Peptide Letters
Volume	14
Issue number	8
DOIs	https://doi.org/10.2174/092986607781483741
Publication status	Published - Aug 1 2007

All Science Journal Classification (ASJC) codes

Structural Biology
Biochemistry

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abstract = "For biophysical studies using heteronuclear NMR analysis of amyloid beta peptide, construction of an efficient and high yield expression system of uniformly isotopic labeled amyloid beta peptide is desirable. Here we succeeded in obtaining 15N-labeled amyloid beta 1-40 expressed by attachment to hen egg white lysozyme as a fusion protein.",

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Expression and purification of uniformly ¹⁵N-labeled amyloid β peptide 1-40 in Escherichia coli

Abstract

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