Molecular Playground/Caspase-7 Dynamics: Difference between revisions

No edit summary
No edit summary
Line 1: Line 1:
Caspases are a family of [[CBI Molecules]] being studied in the  <span class="plainlinks">[http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program]</span> at UMass Amherst and on display at the <span class="plainlinks">[http://www.molecularplayground.org/ Molecular Playground]</span>.
Caspases are a family of [[CBI Molecules]] being studied in the  <span class="plainlinks">[http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program]</span> at UMass Amherst and on display at the <span class="plainlinks">[http://www.molecularplayground.org/ Molecular Playground]</span>.


=== Caspase-7 as studied in <span class="plainlinks">[http://www.chem.umass.edu/~jhardy/ the Hardy Lab] </span>===
=== Caspase-7 as studied in <span class="plainlinks">[http://www.chem.umass.edu/~jhardy/ the Hardy Lab] </span>===
Line 14: Line 16:
*<scene name='Molecular_Playground/Caspase_Dynamics/Morph2/2'>Conformational change between substrate bound and substrate incompatible forms</scene> of Caspase-7.
*<scene name='Molecular_Playground/Caspase_Dynamics/Morph2/2'>Conformational change between substrate bound and substrate incompatible forms</scene> of Caspase-7.


=== Molecular Playground banner ===
=== Molecular Playground banner for Caspase-7 ===


'''Molecular Playground banner:''' Conformational Dynamics between active and allosterically inhibited caspase-7 elucidate the mechanism of allostery in this important class of cysteine proteases.
'''Molecular Playground banner:''' Conformational Dynamics between active and allosterically inhibited caspase-7 elucidate the mechanism of allostery in this important class of cysteine proteases.

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Daniel Seeman, David Canner, Michal Harel, Maureen E. Hill