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George H Lorimer

Showing results (11-20 of 38) with videos related to

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Proceedings of the National Academy of Sciences of the United States of America|November 8, 2008
Setting the chaperonin timer: a two-stroke, two-speed, protein machineJohn P Grason, Jennifer S Gresham, George H Lorimer
Protein Science : a Publication of the Protein Society|December 4, 2004
Identifying natural substrates for chaperonins using a sequence-based approachGeorge Stan, Bernard R Brooks, George H Lorimer, et al.
Biophysical Chemistry|March 21, 2003
Annealing function of GroEL: structural and bioinformatic analysisGeorge Stan, D Thirumalai, George H Lorimer, et al.
Proceedings of the National Academy of Sciences of the United States of America|May 15, 2007
Coupling between allosteric transitions in GroEL and assisted folding of a substrate proteinGeorge Stan, George H Lorimer, D Thirumalai, et al.
Plant, Cell & Environment|January 24, 2018
Rubisco is not really so badCamille Bathellier, Guillaume Tcherkez, George H Lorimer, et al.
Proceedings of the National Academy of Sciences of the United States of America|August 20, 2014
Formation and structures of GroEL:GroES2 chaperonin footballs, the protein-folding functional formXue Fei, Xiang Ye, Nicole A LaRonde, et al.
Proceedings of the National Academy of Sciences of the United States of America|March 16, 2006
Residues in substrate proteins that interact with GroEL in the capture process are buried in the native stateGeorge Stan, Bernard R Brooks, George H Lorimer, et al.
Proceedings of the National Academy of Sciences of the United States of America|July 18, 2013
Crystal structure of a GroEL-ADP complex in the relaxed allosteric state at 2.7 Å resolutionXue Fei, Dong Yang, Nicole LaRonde-LeBlanc, et al.
Chemical Reviews|April 25, 2019
Symmetry, Rigidity, and Allosteric Signaling: From Monomeric Proteins to Molecular MachinesD Thirumalai, Changbong Hyeon, Pavel I Zhuravlev, et al.
Proceedings of the National Academy of Sciences of the United States of America|December 9, 2017
Molecular chaperones maximize the native state yield on biological times by driving substrates out of equilibriumShaon Chakrabarti, Changbong Hyeon, Xiang Ye, et al.
Pageof 4

Showing results (11-20 of 38) with videos related to

Sort By:
Pageof 4
Proceedings of the National Academy of Sciences of the United States of America|November 8, 2008
Setting the chaperonin timer: a two-stroke, two-speed, protein machineJohn P Grason, Jennifer S Gresham, George H Lorimer
Protein Science : a Publication of the Protein Society|December 4, 2004
Identifying natural substrates for chaperonins using a sequence-based approachGeorge Stan, Bernard R Brooks, George H Lorimer, et al.
Biophysical Chemistry|March 21, 2003
Annealing function of GroEL: structural and bioinformatic analysisGeorge Stan, D Thirumalai, George H Lorimer, et al.
Proceedings of the National Academy of Sciences of the United States of America|May 15, 2007
Coupling between allosteric transitions in GroEL and assisted folding of a substrate proteinGeorge Stan, George H Lorimer, D Thirumalai, et al.
Plant, Cell & Environment|January 24, 2018
Rubisco is not really so badCamille Bathellier, Guillaume Tcherkez, George H Lorimer, et al.
Proceedings of the National Academy of Sciences of the United States of America|August 20, 2014
Formation and structures of GroEL:GroES2 chaperonin footballs, the protein-folding functional formXue Fei, Xiang Ye, Nicole A LaRonde, et al.
Proceedings of the National Academy of Sciences of the United States of America|March 16, 2006
Residues in substrate proteins that interact with GroEL in the capture process are buried in the native stateGeorge Stan, Bernard R Brooks, George H Lorimer, et al.
Proceedings of the National Academy of Sciences of the United States of America|July 18, 2013
Crystal structure of a GroEL-ADP complex in the relaxed allosteric state at 2.7 Å resolutionXue Fei, Dong Yang, Nicole LaRonde-LeBlanc, et al.
Chemical Reviews|April 25, 2019
Symmetry, Rigidity, and Allosteric Signaling: From Monomeric Proteins to Molecular MachinesD Thirumalai, Changbong Hyeon, Pavel I Zhuravlev, et al.
Proceedings of the National Academy of Sciences of the United States of America|December 9, 2017
Molecular chaperones maximize the native state yield on biological times by driving substrates out of equilibriumShaon Chakrabarti, Changbong Hyeon, Xiang Ye, et al.
Pageof 4