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BMC Structural Biology
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October 9, 2008
Identification of new, well-populated amino-acid sidechain rotamers involving hydroxyl-hydrogen atoms and sulfhydryl-hydrogen atoms
Bosco K Ho, David A Agard
Bio-Protocol
|
November 7, 2017
Protein Expression and Purification of the Hsp90-Cdc37-Cdk4 Kinase Complex from <i>Saccharomyces cerevisiae</i>
Kliment A Verba, David A Agard
Biochemistry
|
November 12, 2003
Interdependent folding of the N- and C-terminal domains defines the cooperative folding of alpha-lytic protease
Erin L Cunningham, David A Agard
Molecular Cell
|
December 9, 2008
Species-dependent ensembles of conserved conformational states define the Hsp90 chaperone ATPase cycle
Daniel R Southworth, David A Agard
Plos One
|
October 8, 2010
An improved strategy for generating forces in steered molecular dynamics: the mechanical unfolding of titin, e2lip3 and ubiquitin
Bosco K Ho, David A Agard
Protein Science : a Publication of the Protein Society
|
January 24, 2004
Disabling the folding catalyst is the last critical step in alpha-lytic protease folding
Erin L Cunningham, David A Agard
Protein Science : a Publication of the Protein Society
|
January 7, 2010
Conserved tertiary couplings stabilize elements in the PDZ fold, leading to characteristic patterns of domain conformational flexibility
Bosco K Ho, David A Agard
Ultramicroscopy
|
May 12, 2005
Use of surface affinity enrichment and cryo-embedding to prepare in vitro reconstituted mitotic chromosomes for EM tomography
Peter König, Michael Braunfeld, David A Agard
Proteins
|
July 27, 2005
The folding landscape of an alpha-lytic protease variant reveals the role of a conserved beta-hairpin in the development of kinetic stability
Stephanie M E Truhlar, David A Agard
Journal of Chemical Theory and Computation
|
January 11, 2018
The Structural Asymmetry of Mitochondrial Hsp90 (Trap1) Determines Fine Tuning of Functional Dynamics
Elisabetta Moroni, David A Agard, Giorgio Colombo
Page
of 18
Search research articles
Search
Showing results (11-20 of 174) with videos related to
Sort By:
Page
of 18
BMC Structural Biology
|
October 9, 2008
Identification of new, well-populated amino-acid sidechain rotamers involving hydroxyl-hydrogen atoms and sulfhydryl-hydrogen atoms
Bosco K Ho, David A Agard
Bio-Protocol
|
November 7, 2017
Protein Expression and Purification of the Hsp90-Cdc37-Cdk4 Kinase Complex from <i>Saccharomyces cerevisiae</i>
Kliment A Verba, David A Agard
Biochemistry
|
November 12, 2003
Interdependent folding of the N- and C-terminal domains defines the cooperative folding of alpha-lytic protease
Erin L Cunningham, David A Agard
Molecular Cell
|
December 9, 2008
Species-dependent ensembles of conserved conformational states define the Hsp90 chaperone ATPase cycle
Daniel R Southworth, David A Agard
Plos One
|
October 8, 2010
An improved strategy for generating forces in steered molecular dynamics: the mechanical unfolding of titin, e2lip3 and ubiquitin
Bosco K Ho, David A Agard
Protein Science : a Publication of the Protein Society
|
January 24, 2004
Disabling the folding catalyst is the last critical step in alpha-lytic protease folding
Erin L Cunningham, David A Agard
Protein Science : a Publication of the Protein Society
|
January 7, 2010
Conserved tertiary couplings stabilize elements in the PDZ fold, leading to characteristic patterns of domain conformational flexibility
Bosco K Ho, David A Agard
Ultramicroscopy
|
May 12, 2005
Use of surface affinity enrichment and cryo-embedding to prepare in vitro reconstituted mitotic chromosomes for EM tomography
Peter König, Michael Braunfeld, David A Agard
Proteins
|
July 27, 2005
The folding landscape of an alpha-lytic protease variant reveals the role of a conserved beta-hairpin in the development of kinetic stability
Stephanie M E Truhlar, David A Agard
Journal of Chemical Theory and Computation
|
January 11, 2018
The Structural Asymmetry of Mitochondrial Hsp90 (Trap1) Determines Fine Tuning of Functional Dynamics
Elisabetta Moroni, David A Agard, Giorgio Colombo
Page
of 18