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Expression and Purification of Uniformly 15N-Labeled Amyloid β Peptide 1-40 in Escherichia coli

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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.





Keywords: Alzheimer's disiease; Escherichia coli; NMR; amyloid fibrils; amyloid β 1-40; recombinant protein

Document Type: Research Article

DOI: http://dx.doi.org/10.2174/092986607781483741

Publication date: August 1, 2007

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.

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