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C Robert Matthews

Showing results (31-40 of 59) with videos related to

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Journal of the American Chemical Society|January 9, 2013
Interplay between drying and stability of a TIM barrel protein: a combined simulation-experimental studyPayel Das, Divya Kapoor, Kevin T Halloran, et al.
Nature Communications|March 7, 2017
Correlation of fitness landscapes from three orthologous TIM barrels originates from sequence and structure constraintsYvonne H Chan, Sergey V Venev, Konstantin B Zeldovich, et al.
Journal of Molecular Biology|March 24, 2005
An obligatory intermediate controls the folding of the alpha-subunit of tryptophan synthase, a TIM barrel proteinPatrick L Wintrode, Teerapat Rojsajjakul, Ramakrishna Vadrevu, et al.
Protein Engineering, Design & Selection : PEDS|February 3, 2006
The relationship between chain connectivity and domain stability in the equilibrium and kinetic folding mechanisms of dihydrofolate reductase from E.coliAnna-Karin E Svensson, Jill A Zitzewitz, C Robert Matthews, et al.
Journal of Molecular Biology|October 15, 2014
Non-native structure appears in microseconds during the folding of E. coli RNase HLaura E Rosen, Sagar V Kathuria, C Robert Matthews, et al.
Journal of Molecular Biology|March 3, 2007
Microsecond hydrophobic collapse in the folding of Escherichia coli dihydrofolate reductase, an alpha/beta-type proteinMunehito Arai, Elena Kondrashkina, Can Kayatekin, et al.
Biochemistry|September 14, 2020
Trifluoroethanol Partially Unfolds G93A SOD1 Leading to Protein Aggregation: A Study by Native Mass Spectrometry and FPOP Protein FootprintingBen Niu, Brian C Mackness, Jill A Zitzewitz, et al.
Journal of Molecular Biology|October 19, 2007
Structural analysis of kinetic folding intermediates for a TIM barrel protein, indole-3-glycerol phosphate synthase, by hydrogen exchange mass spectrometry and Gō model simulationZhenyu Gu, Maithreyi K Rao, William R Forsyth, et al.
Journal of Molecular Biology|October 19, 2006
Mapping the folding free energy surface for metal-free human Cu,Zn superoxide dismutaseAnna-Karin E Svensson, Osman Bilsel, Elena Kondrashkina, et al.
Protein Science : a Publication of the Protein Society|December 15, 2015
Clusters of isoleucine, leucine, and valine side chains define cores of stability in high-energy states of globular proteins: Sequence determinants of structure and stabilitySagar V Kathuria, Yvonne H Chan, R Paul Nobrega, et al.
Pageof 6

Showing results (31-40 of 59) with videos related to

Sort By:
Pageof 6
Journal of the American Chemical Society|January 9, 2013
Interplay between drying and stability of a TIM barrel protein: a combined simulation-experimental studyPayel Das, Divya Kapoor, Kevin T Halloran, et al.
Nature Communications|March 7, 2017
Correlation of fitness landscapes from three orthologous TIM barrels originates from sequence and structure constraintsYvonne H Chan, Sergey V Venev, Konstantin B Zeldovich, et al.
Journal of Molecular Biology|March 24, 2005
An obligatory intermediate controls the folding of the alpha-subunit of tryptophan synthase, a TIM barrel proteinPatrick L Wintrode, Teerapat Rojsajjakul, Ramakrishna Vadrevu, et al.
Protein Engineering, Design & Selection : PEDS|February 3, 2006
The relationship between chain connectivity and domain stability in the equilibrium and kinetic folding mechanisms of dihydrofolate reductase from E.coliAnna-Karin E Svensson, Jill A Zitzewitz, C Robert Matthews, et al.
Journal of Molecular Biology|October 15, 2014
Non-native structure appears in microseconds during the folding of E. coli RNase HLaura E Rosen, Sagar V Kathuria, C Robert Matthews, et al.
Journal of Molecular Biology|March 3, 2007
Microsecond hydrophobic collapse in the folding of Escherichia coli dihydrofolate reductase, an alpha/beta-type proteinMunehito Arai, Elena Kondrashkina, Can Kayatekin, et al.
Biochemistry|September 14, 2020
Trifluoroethanol Partially Unfolds G93A SOD1 Leading to Protein Aggregation: A Study by Native Mass Spectrometry and FPOP Protein FootprintingBen Niu, Brian C Mackness, Jill A Zitzewitz, et al.
Journal of Molecular Biology|October 19, 2007
Structural analysis of kinetic folding intermediates for a TIM barrel protein, indole-3-glycerol phosphate synthase, by hydrogen exchange mass spectrometry and Gō model simulationZhenyu Gu, Maithreyi K Rao, William R Forsyth, et al.
Journal of Molecular Biology|October 19, 2006
Mapping the folding free energy surface for metal-free human Cu,Zn superoxide dismutaseAnna-Karin E Svensson, Osman Bilsel, Elena Kondrashkina, et al.
Protein Science : a Publication of the Protein Society|December 15, 2015
Clusters of isoleucine, leucine, and valine side chains define cores of stability in high-energy states of globular proteins: Sequence determinants of structure and stabilitySagar V Kathuria, Yvonne H Chan, R Paul Nobrega, et al.
Pageof 6