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C M Dobson

Showing results (211-220 of 271) with videos related to

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Protein Science : a Publication of the Protein Society|September 7, 2000
Initial denaturing conditions influence the slow folding phase of acylphosphatase associated with proline isomerizationT A Pertinhez, D Hamada, L J Smith, et al.
Protein Science : a Publication of the Protein Society|December 1, 1996
Thermal stability of the three domains of streptokinase studied by circular dichroism and nuclear magnetic resonanceF Conejero-Lara, J Parrado, A I Azuaga, et al.
Journal of Molecular Biology|May 18, 1999
Rapid collapse and slow structural reorganisation during the refolding of bovine alpha-lactalbuminV Forge, R T Wijesinha, J Balbach, et al.
Biochemistry|June 3, 1999
Mechanistic studies of the folding of human lysozyme and the origin of amyloidogenic behavior in its disease-related variantsD Canet, M Sunde, A M Last, et al.
Proceedings of the National Academy of Sciences of the United States of America|July 8, 1997
Detection of residue contacts in a protein folding intermediateJ Balbach, V Forge, W S Lau, et al.
Protein Science : a Publication of the Protein Society|April 1, 1996
The domain organization of streptokinase: nuclear magnetic resonance, circular dichroism, and functional characterization of proteolytic fragmentsJ Parrado, F Conejero-Lara, R A Smith, et al.
Biochemistry|February 23, 1999
Thermodynamics and kinetics of folding of common-type acylphosphatase: comparison to the highly homologous muscle isoenzymeN Taddei, F Chiti, P Paoli, et al.
Proceedings of the National Academy of Sciences of the United States of America|September 15, 1991
Antigen mobility in the combining site of an anti-peptide antibodyJ C Cheetham, D P Raleigh, R E Griest, et al.
Journal of Molecular Biology|October 29, 1998
Structural characterization of the transition state for folding of muscle acylphosphataseF Chiti, N Taddei, N A van Nuland, et al.
Protein Engineering|September 18, 1998
Studies on enzymatic activity and conformational stability of muscle acylphosphatase mutated at conserved lysine residuesF Chiti, F Magherini, N Taddei, et al.
Pageof 28

Showing results (211-220 of 271) with videos related to

Sort By:
Pageof 28
Protein Science : a Publication of the Protein Society|September 7, 2000
Initial denaturing conditions influence the slow folding phase of acylphosphatase associated with proline isomerizationT A Pertinhez, D Hamada, L J Smith, et al.
Protein Science : a Publication of the Protein Society|December 1, 1996
Thermal stability of the three domains of streptokinase studied by circular dichroism and nuclear magnetic resonanceF Conejero-Lara, J Parrado, A I Azuaga, et al.
Journal of Molecular Biology|May 18, 1999
Rapid collapse and slow structural reorganisation during the refolding of bovine alpha-lactalbuminV Forge, R T Wijesinha, J Balbach, et al.
Biochemistry|June 3, 1999
Mechanistic studies of the folding of human lysozyme and the origin of amyloidogenic behavior in its disease-related variantsD Canet, M Sunde, A M Last, et al.
Proceedings of the National Academy of Sciences of the United States of America|July 8, 1997
Detection of residue contacts in a protein folding intermediateJ Balbach, V Forge, W S Lau, et al.
Protein Science : a Publication of the Protein Society|April 1, 1996
The domain organization of streptokinase: nuclear magnetic resonance, circular dichroism, and functional characterization of proteolytic fragmentsJ Parrado, F Conejero-Lara, R A Smith, et al.
Biochemistry|February 23, 1999
Thermodynamics and kinetics of folding of common-type acylphosphatase: comparison to the highly homologous muscle isoenzymeN Taddei, F Chiti, P Paoli, et al.
Proceedings of the National Academy of Sciences of the United States of America|September 15, 1991
Antigen mobility in the combining site of an anti-peptide antibodyJ C Cheetham, D P Raleigh, R E Griest, et al.
Journal of Molecular Biology|October 29, 1998
Structural characterization of the transition state for folding of muscle acylphosphataseF Chiti, N Taddei, N A van Nuland, et al.
Protein Engineering|September 18, 1998
Studies on enzymatic activity and conformational stability of muscle acylphosphatase mutated at conserved lysine residuesF Chiti, F Magherini, N Taddei, et al.
Pageof 28