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Science (New York, N.Y.)|November 15, 1996
Protein folding monitored at individual residues during a two-dimensional NMR experimentJ Balbach, V Forge, W S Lau, et al.Journal of Molecular Biology|May 18, 1999
Rapid collapse and slow structural reorganisation during the refolding of bovine alpha-lactalbuminV Forge, R T Wijesinha, J Balbach, et al.Proceedings of the National Academy of Sciences of the United States of America|July 8, 1997
Detection of residue contacts in a protein folding intermediateJ Balbach, V Forge, W S Lau, et al.Journal of Biomolecular NMR|May 29, 2000
Probing hydrogen bonds in the antibody-bound HIV-1 gp120 V3 loop by solid state NMR REDOR measurementsJ J Balbach, J Yang, D P Weliky, et al.Nature Structural Biology|October 1, 1995
Following protein folding in real time using NMR spectroscopyJ Balbach, V Forge, N A van Nuland, et al.Proceedings of the National Academy of Sciences of the United States of America|December 14, 2002
A structural model for Alzheimer's beta -amyloid fibrils based on experimental constraints from solid state NMRAneta T Petkova, Yoshitaka Ishii, John J Balbach, et al.Biophysical Journal|July 19, 2002
Supramolecular structure in full-length Alzheimer's beta-amyloid fibrils: evidence for a parallel beta-sheet organization from solid-state nuclear magnetic resonanceJohn J Balbach, Aneta T Petkova, Nathan A Oyler, et al.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.Deutsche Medizinische Wochenschrift (1946)|February 7, 1975
[Clinical studies on the effect of drugs used in the treatment of angina]B Härich, R Hassis, H Immich, 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.Pageof 5