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- W2003106467 endingPage "693" @default.
- W2003106467 startingPage "681" @default.
- W2003106467 abstract "Two synthetic peptides from the beta 2 subunit of tryptophan synthase have been studied by 1H-NMR spectroscopy at 300 MHz. One peptide, His-Gly-Arg-Val-Gly-Ile-Tyr-Phe-Gly-Met-Lys (peptide 11; Ile, isoleucine) is antigenic and binds with a high affinity to a monoclonal antibody that recognizes the native beta 2 subunit. The second peptide, His-Gly-Arg-Val-Gly-Ile-Tyr-Phe (peptide 8) reacts very weakly with the antibody. The 1H-NMR spectra of the two peptides have been assigned from two-dimensional techniques in H2O, 2H2O and (2H6) dimethyl sulfoxide [(2H6)Me2SO]. The structure has been evaluated through analysis of nuclear Overhauser effects, coupling constants, amide-proton exchange rates and their temperature coefficients, and chemical shifts. In aqueous solvent, the C-terminal part of peptide 11 presents some structure centered around residues Phe-Gly-Met. The relationship between the structure found in peptide 11 and its antigenic nature is discussed." @default.
- W2003106467 created "2016-06-24" @default.
- W2003106467 creator A5000077022 @default.
- W2003106467 creator A5002217794 @default.
- W2003106467 creator A5005071676 @default.
- W2003106467 creator A5072693404 @default.
- W2003106467 date "1991-11-01" @default.
- W2003106467 modified "2023-09-24" @default.
- W2003106467 title "1H-NMR conformational analysis of a high-affinity antigenic 11-residue peptide from the tryptophan synthase beta2 subunit" @default.
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