Search research articles
Contact Us
Filters
Showing results (31-40 of 62) with videos related to
Page
of 7
Sort By:
Journal of the American Chemical Society
|
October 10, 2002
Solution NMR techniques for large molecular and supramolecular structures
Roland Riek, Jocelyne Fiaux, Eric B Bertelsen, et al.
Journal of Molecular Biology
|
November 28, 2012
Structure and allostery of the chaperonin GroEL
Helen 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 system
Andrew 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 solution
Reto 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 GroEL
Fumihiro 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 translocation
Jörg 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 GroEL
Reto 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 structures
Reto 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 chaperonin
Ramanathan 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 state
Eli Chapman, George W Farr, Wayne A Fenton, et al.
Page
of 7
Search research articles
Search
Showing results (31-40 of 62) with videos related to
Sort By:
Page
of 7
Journal of the American Chemical Society
|
October 10, 2002
Solution NMR techniques for large molecular and supramolecular structures
Roland Riek, Jocelyne Fiaux, Eric B Bertelsen, et al.
Journal of Molecular Biology
|
November 28, 2012
Structure and allostery of the chaperonin GroEL
Helen 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 system
Andrew 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 solution
Reto 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 GroEL
Fumihiro 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 translocation
Jörg 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 GroEL
Reto 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 structures
Reto 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 chaperonin
Ramanathan 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 state
Eli Chapman, George W Farr, Wayne A Fenton, et al.
Page
of 7