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J P Waltho

Showing results (1-10 of 39) with videos related to

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Biochemical Pharmacology|January 1, 1988
Molecular basis of the activity of antibiotics of the vancomycin groupD H Williams, J P Waltho
Ciba Foundation Symposium|January 1, 1991
The natural design of vancomycin family antibiotics to bind their target peptidesJ P Waltho, D H Williams
Current Opinion in Biotechnology|August 1, 1997
Protein folding and intermediatesA R Clarke, J P Waltho
Biochemical Society Transactions|August 28, 2002
Amyloid fibril formation by human stefin B: influence of the initial pH-induced intermediate stateE Zerovnik, V Turk, J P Waltho
Methods in Molecular Biology (Clifton, N.J.)|January 1, 1997
Double and triple resonance NMR methods for protein assignmentB Whitehead, C J Craven, J P Waltho
Journal of Computer-Aided Molecular Design|April 1, 1988
Forces in molecular recognition: comparison of experimental data and molecular mechanics calculationsJ P Waltho, J G Vinter, A Davis, et al.
Proteins|August 26, 1998
On the mechanism of human stefin B folding: I. Comparison to homologous stefin A. Influence of pH and trifluoroethanol on the fast and slow folding phasesE Zerovnik, R Virden, R Jerala, et al.
Biochemistry. Biokhimiia|November 20, 2012
Reflections on biocatalysis involving phosphorusG M Blackburn, M W Bowler, Yi Jin, et al.
FEBS Letters|July 3, 1989
Conformation of a T cell stimulating peptide in aqueous solutionJ P Waltho, V A Feher, R A Lerner, et al.
Journal of Molecular Biology|January 8, 1999
Characterisation of low free-energy excited states of folded proteinsN J Baxter, L L Hosszu, J P Waltho, et al.
Pageof 4

Showing results (1-10 of 39) with videos related to

Sort By:
Pageof 4
Biochemical Pharmacology|January 1, 1988
Molecular basis of the activity of antibiotics of the vancomycin groupD H Williams, J P Waltho
Ciba Foundation Symposium|January 1, 1991
The natural design of vancomycin family antibiotics to bind their target peptidesJ P Waltho, D H Williams
Current Opinion in Biotechnology|August 1, 1997
Protein folding and intermediatesA R Clarke, J P Waltho
Biochemical Society Transactions|August 28, 2002
Amyloid fibril formation by human stefin B: influence of the initial pH-induced intermediate stateE Zerovnik, V Turk, J P Waltho
Methods in Molecular Biology (Clifton, N.J.)|January 1, 1997
Double and triple resonance NMR methods for protein assignmentB Whitehead, C J Craven, J P Waltho
Journal of Computer-Aided Molecular Design|April 1, 1988
Forces in molecular recognition: comparison of experimental data and molecular mechanics calculationsJ P Waltho, J G Vinter, A Davis, et al.
Proteins|August 26, 1998
On the mechanism of human stefin B folding: I. Comparison to homologous stefin A. Influence of pH and trifluoroethanol on the fast and slow folding phasesE Zerovnik, R Virden, R Jerala, et al.
Biochemistry. Biokhimiia|November 20, 2012
Reflections on biocatalysis involving phosphorusG M Blackburn, M W Bowler, Yi Jin, et al.
FEBS Letters|July 3, 1989
Conformation of a T cell stimulating peptide in aqueous solutionJ P Waltho, V A Feher, R A Lerner, et al.
Journal of Molecular Biology|January 8, 1999
Characterisation of low free-energy excited states of folded proteinsN J Baxter, L L Hosszu, J P Waltho, et al.
Pageof 4