Search research articles
Contact Us
Filters
Showing results (11-20 of 21) with videos related to
Page
of 3
Sort By:
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 study
C 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 inhibitor
C 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 inhibitor
J 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 inhibitor
C 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 measurements
C 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 inhibitor
N 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 intermediate
C P van Mierlo, W M van Dongen, F Vergeldt, et al.
European Journal of Biochemistry
|
November 26, 1990
Tertiary structure of two-electron reduced Megasphaera elsdenii flavodoxin and some implications, as determined by two-dimensional 1H-NMR and restrained molecular dynamics
C P van Mierlo, P Lijnzaad, J Vervoort, et al.
European Journal of Biochemistry
|
November 26, 1990
A two-dimensional 1H-NMR study on Megasphaera elsdenii flavodoxin in the oxidized state and some comparisons with the two-electron-reduced state
C P van Mierlo, B P van der Sanden, P van Woensel, et al.
Page
of 3
Search research articles
Search
Showing results (11-20 of 21) with videos related to
Sort By:
Page
of 3
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 study
C 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 inhibitor
C 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 inhibitor
J 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 inhibitor
C 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 measurements
C 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 inhibitor
N 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 intermediate
C P van Mierlo, W M van Dongen, F Vergeldt, et al.
European Journal of Biochemistry
|
November 26, 1990
Tertiary structure of two-electron reduced Megasphaera elsdenii flavodoxin and some implications, as determined by two-dimensional 1H-NMR and restrained molecular dynamics
C P van Mierlo, P Lijnzaad, J Vervoort, et al.
European Journal of Biochemistry
|
November 26, 1990
A two-dimensional 1H-NMR study on Megasphaera elsdenii flavodoxin in the oxidized state and some comparisons with the two-electron-reduced state
C P van Mierlo, B P van der Sanden, P van Woensel, et al.
Page
of 3