Biological NMR spectroscopy
Biomolecules Nuclear magnetic resonance spectroscopy SCIENCE Magnetic Resonance Spectroscopy Molecular Biology sähkökirjat
Oxford University Press
1997
EISBN 9780195357424
Simple insights from the beginnings of magnetic resonance in molecular biology / O. Jardetzky.
Choice of problems in the early days of biological NMR spectroscopy / M. Cohn.
Early days of biochemical NMR / R.G. Shulman.
William D. Phillips memorial lecture / J.J.H. Ackerman.
Flexibility and function of the escherichia coli trp repressor / M.R. Gryk and O. Jardetzky.
Heteronuclear strategies for the assignment of larger protein/DNA complexes : application to the 37 kDa trp repressor-operator complex / M.J. Revington, W. Lee, and C.H. Arrowsmith.
Design of novel hemoglobins / C. Ho and H.-W. Kim.
The role of NMR spectroscopy in understanding how proteins fold / C.M. Dobson.
NMR approaches to understanding protein specificity / G.C.K. Roberts ... [et al.].
NMR and mutagenesis investigations of a model cis:trans peptide isomerzation reaction : Xaa¹¹ ¹
This text presents a critical assessment of progress on the use of nuclear magnetic resonance (NMR) spectroscopy to determine the structure of proteins, including brief reviews of the history of the field along with coverage of current clinical and in vivo applications.
Choice of problems in the early days of biological NMR spectroscopy / M. Cohn.
Early days of biochemical NMR / R.G. Shulman.
William D. Phillips memorial lecture / J.J.H. Ackerman.
Flexibility and function of the escherichia coli trp repressor / M.R. Gryk and O. Jardetzky.
Heteronuclear strategies for the assignment of larger protein/DNA complexes : application to the 37 kDa trp repressor-operator complex / M.J. Revington, W. Lee, and C.H. Arrowsmith.
Design of novel hemoglobins / C. Ho and H.-W. Kim.
The role of NMR spectroscopy in understanding how proteins fold / C.M. Dobson.
NMR approaches to understanding protein specificity / G.C.K. Roberts ... [et al.].
NMR and mutagenesis investigations of a model cis:trans peptide isomerzation reaction : Xaa¹¹ ¹
This text presents a critical assessment of progress on the use of nuclear magnetic resonance (NMR) spectroscopy to determine the structure of proteins, including brief reviews of the history of the field along with coverage of current clinical and in vivo applications.
