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Arthur L Horwich

Showing results (31-40 of 62) with videos related to

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Journal of the American Chemical Society|October 10, 2002
Solution NMR techniques for large molecular and supramolecular structuresRoland Riek, Jocelyne Fiaux, Eric B Bertelsen, et al.
Journal of Molecular Biology|November 28, 2012
Structure and allostery of the chaperonin GroELHelen R Saibil, Wayne A Fenton, Daniel K Clare, et al.
FEBS Letters|January 21, 2015
Unfolded DapA forms aggregates when diluted into free solution, confounding comparison with folding by the GroEL/GroES chaperonin systemAndrew Ambrose, Wayne Fenton, Damian J Mason, et al.
Proceedings of the National Academy of Sciences of the United States of America|December 21, 2007
Folding trajectories of human dihydrofolate reductase inside the GroEL GroES chaperonin cavity and free in solutionReto Horst, Wayne A Fenton, S Walter Englander, et al.
Proceedings of the National Academy of Sciences of the United States of America|October 14, 2004
Substrate polypeptide presents a load on the apical domains of the chaperonin GroELFumihiro Motojima, Charu Chaudhry, Wayne A Fenton, et al.
Cell|July 2, 2005
Loops in the central channel of ClpA chaperone mediate protein binding, unfolding, and translocationJörg Hinnerwisch, Wayne A Fenton, Krystyna J Furtak, et al.
Proceedings of the National Academy of Sciences of the United States of America|August 24, 2005
Direct NMR observation of a substrate protein bound to the chaperonin GroELReto Horst, Eric B Bertelsen, Jocelyne Fiaux, et al.
Proceedings of the National Academy of Sciences of the United States of America|October 13, 2006
Proton-proton Overhauser NMR spectroscopy with polypeptide chains in large structuresReto Horst, Gerhard Wider, Jocelyne Fiaux, et al.
International Journal of Biological Macromolecules|July 1, 2018
A two-domain folding intermediate of RuBisCO in complex with the GroEL chaperoninRamanathan Natesh, Daniel K Clare, George W Farr, et al.
Proceedings of the National Academy of Sciences of the United States of America|December 4, 2008
Requirement for binding multiple ATPs to convert a GroEL ring to the folding-active stateEli Chapman, George W Farr, Wayne A Fenton, et al.
Pageof 7

Showing results (31-40 of 62) with videos related to

Sort By:
Pageof 7
Journal of the American Chemical Society|October 10, 2002
Solution NMR techniques for large molecular and supramolecular structuresRoland Riek, Jocelyne Fiaux, Eric B Bertelsen, et al.
Journal of Molecular Biology|November 28, 2012
Structure and allostery of the chaperonin GroELHelen R Saibil, Wayne A Fenton, Daniel K Clare, et al.
FEBS Letters|January 21, 2015
Unfolded DapA forms aggregates when diluted into free solution, confounding comparison with folding by the GroEL/GroES chaperonin systemAndrew Ambrose, Wayne Fenton, Damian J Mason, et al.
Proceedings of the National Academy of Sciences of the United States of America|December 21, 2007
Folding trajectories of human dihydrofolate reductase inside the GroEL GroES chaperonin cavity and free in solutionReto Horst, Wayne A Fenton, S Walter Englander, et al.
Proceedings of the National Academy of Sciences of the United States of America|October 14, 2004
Substrate polypeptide presents a load on the apical domains of the chaperonin GroELFumihiro Motojima, Charu Chaudhry, Wayne A Fenton, et al.
Cell|July 2, 2005
Loops in the central channel of ClpA chaperone mediate protein binding, unfolding, and translocationJörg Hinnerwisch, Wayne A Fenton, Krystyna J Furtak, et al.
Proceedings of the National Academy of Sciences of the United States of America|August 24, 2005
Direct NMR observation of a substrate protein bound to the chaperonin GroELReto Horst, Eric B Bertelsen, Jocelyne Fiaux, et al.
Proceedings of the National Academy of Sciences of the United States of America|October 13, 2006
Proton-proton Overhauser NMR spectroscopy with polypeptide chains in large structuresReto Horst, Gerhard Wider, Jocelyne Fiaux, et al.
International Journal of Biological Macromolecules|July 1, 2018
A two-domain folding intermediate of RuBisCO in complex with the GroEL chaperoninRamanathan Natesh, Daniel K Clare, George W Farr, et al.
Proceedings of the National Academy of Sciences of the United States of America|December 4, 2008
Requirement for binding multiple ATPs to convert a GroEL ring to the folding-active stateEli Chapman, George W Farr, Wayne A Fenton, et al.
Pageof 7