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J Balbach

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Biochemistry|November 15, 2000
Amyloid fibril formation by A beta 16-22, a seven-residue fragment of the Alzheimer's beta-amyloid peptide, and structural characterization by solid state NMRJ J Balbach, Y Ishii, O N Antzutkin, et al.
Journal of Molecular Biology|October 11, 2011
Escherichia coli peptide binding protein OppA has a preference for positively charged peptidesM M Klepsch, M Kovermann, C Löw, et al.
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Showing results (21-30 of 22) with videos related to

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You have reached the last page of results.This site can display upto 22 results.
Biochemistry|November 15, 2000
Amyloid fibril formation by A beta 16-22, a seven-residue fragment of the Alzheimer's beta-amyloid peptide, and structural characterization by solid state NMRJ J Balbach, Y Ishii, O N Antzutkin, et al.
Journal of Molecular Biology|October 11, 2011
Escherichia coli peptide binding protein OppA has a preference for positively charged peptidesM M Klepsch, M Kovermann, C Löw, et al.
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