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pro vyhledávání: '"M. D. BRUCH"'
Autor:
M. D. BRUCH, C. DYBOWSKI
Publikováno v:
ChemInform. 27
Publikováno v:
Biopolymers. 36(2)
CD and nmr spectroscopy were used to compare the conformational properties of two related peptides. One of the peptides, Model AB, was designed to adopt a helix-turn-extended strand (alpha beta) tertiary structure in water that might be stabilized by
Autor:
M D, Bruch, L M, Gierasch
Publikováno v:
The Journal of biological chemistry. 265(7)
Previous studies of isolated peptides corresponding to the wild-type signal sequence of the LamB protein of Escherichia coli and to several export-impaired mutants demonstrated that a high tendency to adopt an alpha-helical conformation in low dielec
Publikováno v:
Journal of Biological Chemistry. 257:3409-3413
Individual anomeric protons that are unresolved in the one-dimensional 250-MHz spectra of oligomannosidic glycopeptides can be separated and characterized by two-dimensional J-resolved NMR spectroscopy. Homogeneous preparations of ovalbumin glycopept
Autor:
M. D. Bruch, W. G. Payne
Publikováno v:
Macromolecules. 19:2712-2721
Autor:
M. D. Bruch
Publikováno v:
Macromolecules. 21:2707-2713
Autor:
R C, Bruch, M D, Bruch
Publikováno v:
The Journal of biological chemistry. 257(7)
Individual anomeric protons that are unresolved in the one-dimensional 250-MHz spectra of oligomannosidic glycopeptides can be separated and characterized by two-dimensional J-resolved NMR spectroscopy. Homogeneous preparations of ovalbumin glycopept