Hydrogen exchange in the hydrophilic regions of detergent-solubilized M13 coat protein detected by 13C nuclear magnetic resonance isotope shifts.
暂无分享,去创建一个
[1] N. Kallenbach,et al. Hydrogen exchange and structural dynamics of proteins and nucleic acids , 1983, Quarterly Reviews of Biophysics.
[2] S. Opella,et al. Structural properties of fd coat protein in sodium dodecyl sulfate micelles. , 1980, Biochemical and biophysical research communications.
[3] W. Hull,et al. Qualitative aspects of hydrogen-deuterium exchange in the 1H, 13C, and 15N nuclear magnetic resonance spectra of viomycin in aqueous solution. , 1978, Biochemistry.
[4] R. E. Webster,et al. Evidence for a major conformational change of coat protein in assembly of fl bacteriophage , 1976, Nature.
[5] W. Konigsberg,et al. Reinvestigation of a region of the fd bacteriophage coat protein sequence. , 1974, Journal of molecular biology.
[6] J. Feeney,et al. The assignment of carbon-13 resonances from carbonyl groups in peptides , 1974 .
[7] H. Smilowitz. Bacteriophage f1 Infection: Fate of the Parental Major Coat Protein , 1974, Journal of virology.
[8] H. Kohler,et al. Virusproteine, IV. Die Konstitution des Hüllproteins des Phagen fd , 1969 .