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Biochemical Pharmacology
|
January 1, 1988
Molecular basis of the activity of antibiotics of the vancomycin group
D H Williams, J P Waltho
Ciba Foundation Symposium
|
January 1, 1991
The natural design of vancomycin family antibiotics to bind their target peptides
J P Waltho, D H Williams
Current Opinion in Biotechnology
|
August 1, 1997
Protein folding and intermediates
A 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 state
E Zerovnik, V Turk, J P Waltho
Methods in Molecular Biology (Clifton, N.J.)
|
January 1, 1997
Double and triple resonance NMR methods for protein assignment
B 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 calculations
J 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 phases
E Zerovnik, R Virden, R Jerala, et al.
Biochemistry. Biokhimiia
|
November 20, 2012
Reflections on biocatalysis involving phosphorus
G M Blackburn, M W Bowler, Yi Jin, et al.
FEBS Letters
|
July 3, 1989
Conformation of a T cell stimulating peptide in aqueous solution
J 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 proteins
N J Baxter, L L Hosszu, J P Waltho, et al.
Page
of 4
Search research articles
Search
Showing results (1-10 of 39) with videos related to
Sort By:
Page
of 4
Biochemical Pharmacology
|
January 1, 1988
Molecular basis of the activity of antibiotics of the vancomycin group
D H Williams, J P Waltho
Ciba Foundation Symposium
|
January 1, 1991
The natural design of vancomycin family antibiotics to bind their target peptides
J P Waltho, D H Williams
Current Opinion in Biotechnology
|
August 1, 1997
Protein folding and intermediates
A 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 state
E Zerovnik, V Turk, J P Waltho
Methods in Molecular Biology (Clifton, N.J.)
|
January 1, 1997
Double and triple resonance NMR methods for protein assignment
B 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 calculations
J 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 phases
E Zerovnik, R Virden, R Jerala, et al.
Biochemistry. Biokhimiia
|
November 20, 2012
Reflections on biocatalysis involving phosphorus
G M Blackburn, M W Bowler, Yi Jin, et al.
FEBS Letters
|
July 3, 1989
Conformation of a T cell stimulating peptide in aqueous solution
J 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 proteins
N J Baxter, L L Hosszu, J P Waltho, et al.
Page
of 4