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Biochemistry|September 12, 2001
The ligand-binding loops in the tunicate C-type lectin TC14 are rigidS F Poget, S M Freund, M J Howard, et al.Biochemistry|September 22, 2000
Biophysical characterization of elongin C from Saccharomyces cerevisiaeA Buchberger, M J Howard, S M Freund, et al.Journal of Molecular Biology|June 10, 1998
Characterisation of urea-denatured states of an immunoglobulin superfamily domain by heteronuclear NMRS Fong, M Bycroft, J Clarke, et al.FEBS Letters|April 10, 1995
Assignment of the backbone 1H,15N,13C NMR resonances and secondary structure of a double-stranded RNA binding domain from the Drosophila protein staufenM Bycroft, M Proctor, S M Freund, et al.Journal of Molecular Biology|July 10, 1999
The structure of a tunicate C-type lectin from Polyandrocarpa misakiensis complexed with D -galactoseS F Poget, G B Legge, M R Proctor, et al.Biochemistry|August 2, 1994
Three-dimensional solution structure and 13C assignments of barstar using nuclear magnetic resonance spectroscopyM J Lubienski, M Bycroft, S M Freund, et al.Journal of Molecular Biology|March 13, 2001
The UBX domain: a widespread ubiquitin-like moduleA Buchberger, M J Howard, M Proctor, et al.Cell|January 24, 1997
The solution structure of the S1 RNA binding domain: a member of an ancient nucleic acid-binding foldM Bycroft, T J Hubbard, M Proctor, et al.Proceedings of the National Academy of Sciences of the United States of America|September 27, 1994
Toward solving the folding pathway of barnase: the complete backbone 13C, 15N, and 1H NMR assignments of its pH-denatured stateV L Arcus, S Vuilleumier, S M Freund, et al.Journal of Molecular Biology|November 24, 1995
A comparison of the pH, urea, and temperature-denatured states of barnase by heteronuclear NMR: implications for the initiation of protein foldingV L Arcus, S Vuilleumier, S M Freund, et al.Pageof 12