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P van Mierlo

Showing results (11-20 of 32) with videos related to

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Biochemistry|June 11, 1991
Solution conformation of a peptide fragment representing a proposed RNA-binding site of a viral coat protein studied by two-dimensional NMRM van der Graaf, C P van Mierlo, M A Hemminga
Protein Science : a Publication of the Protein Society|March 30, 2000
Apoflavodoxin (un)folding followed at the residue level by NMRC P van Mierlo, J M van den Oever, E Steensma
European Journal of Biochemistry|January 15, 1996
Redox properties of wild-type, Cys69Ala, and Cys69Ser Azotobacter vinelandii flavodoxin II as measured by cyclic voltammetry and EPR spectroscopy,E Steensma, H A Heering, W R Hagen, et al.
Journal of Molecular Biology|November 20, 1991
(14-38, 30-51) double-disulphide intermediate in folding of bovine pancreatic trypsin inhibitor: a two-dimensional 1H nuclear magnetic resonance studyC P van Mierlo, N J Darby, D Neuhaus, et al.
Journal of Molecular Biology|November 20, 1991
Two-dimensional 1H nuclear magnetic resonance study of the (5-55) single-disulphide folding intermediate of bovine pancreatic trypsin inhibitorC P van Mierlo, N J Darby, D Neuhaus, et al.
Journal of Molecular Biology|March 5, 1993
Local structure due to an aromatic-amide interaction observed by 1H-nuclear magnetic resonance spectroscopy in peptides related to the N terminus of bovine pancreatic trypsin inhibitorJ Kemmink, C P van Mierlo, R M Scheek, et al.
Journal of Molecular Biology|January 21, 1994
1H NMR analysis of the partly-folded non-native two-disulphide intermediates (30-51,5-14) and (30-51,5-38) in the folding pathway of bovine pancreatic trypsin inhibitorC P van Mierlo, J Kemmink, D Neuhaus, et al.
Journal of Molecular Biology|February 20, 1993
Partially folded conformation of the (30-51) intermediate in the disulphide folding pathway of bovine pancreatic trypsin inhibitor. 1H and 15N resonance assignments and determination of backbone dynamics from 15N relaxation measurementsC P van Mierlo, N J Darby, J Keeler, et al.
Journal of Molecular Biology|April 20, 1992
Kinetic roles and conformational properties of the non-native two-disulphide intermediates in the refolding of bovine pancreatic trypsin inhibitorN J Darby, C P van Mierlo, G H Scott, et al.
Protein Science : a Publication of the Protein Society|November 25, 1998
The equilibrium unfolding of Azotobacter vinelandii apoflavodoxin II occurs via a relatively stable folding intermediateC P van Mierlo, W M van Dongen, F Vergeldt, et al.
Pageof 4

Showing results (11-20 of 32) with videos related to

Sort By:
Pageof 4
Biochemistry|June 11, 1991
Solution conformation of a peptide fragment representing a proposed RNA-binding site of a viral coat protein studied by two-dimensional NMRM van der Graaf, C P van Mierlo, M A Hemminga
Protein Science : a Publication of the Protein Society|March 30, 2000
Apoflavodoxin (un)folding followed at the residue level by NMRC P van Mierlo, J M van den Oever, E Steensma
European Journal of Biochemistry|January 15, 1996
Redox properties of wild-type, Cys69Ala, and Cys69Ser Azotobacter vinelandii flavodoxin II as measured by cyclic voltammetry and EPR spectroscopy,E Steensma, H A Heering, W R Hagen, et al.
Journal of Molecular Biology|November 20, 1991
(14-38, 30-51) double-disulphide intermediate in folding of bovine pancreatic trypsin inhibitor: a two-dimensional 1H nuclear magnetic resonance studyC P van Mierlo, N J Darby, D Neuhaus, et al.
Journal of Molecular Biology|November 20, 1991
Two-dimensional 1H nuclear magnetic resonance study of the (5-55) single-disulphide folding intermediate of bovine pancreatic trypsin inhibitorC P van Mierlo, N J Darby, D Neuhaus, et al.
Journal of Molecular Biology|March 5, 1993
Local structure due to an aromatic-amide interaction observed by 1H-nuclear magnetic resonance spectroscopy in peptides related to the N terminus of bovine pancreatic trypsin inhibitorJ Kemmink, C P van Mierlo, R M Scheek, et al.
Journal of Molecular Biology|January 21, 1994
1H NMR analysis of the partly-folded non-native two-disulphide intermediates (30-51,5-14) and (30-51,5-38) in the folding pathway of bovine pancreatic trypsin inhibitorC P van Mierlo, J Kemmink, D Neuhaus, et al.
Journal of Molecular Biology|February 20, 1993
Partially folded conformation of the (30-51) intermediate in the disulphide folding pathway of bovine pancreatic trypsin inhibitor. 1H and 15N resonance assignments and determination of backbone dynamics from 15N relaxation measurementsC P van Mierlo, N J Darby, J Keeler, et al.
Journal of Molecular Biology|April 20, 1992
Kinetic roles and conformational properties of the non-native two-disulphide intermediates in the refolding of bovine pancreatic trypsin inhibitorN J Darby, C P van Mierlo, G H Scott, et al.
Protein Science : a Publication of the Protein Society|November 25, 1998
The equilibrium unfolding of Azotobacter vinelandii apoflavodoxin II occurs via a relatively stable folding intermediateC P van Mierlo, W M van Dongen, F Vergeldt, et al.
Pageof 4