Event Title
Tertiary Structure and Active Sites Conformations in Forms I and II RuBisCO
Location
Parker-Reed, SSWAC
Start Date
30-4-2015 11:00 AM
End Date
30-4-2015 1:55 PM
Project Type
Poster
Description
A slow catalytic rate and poor substrate discrimination are contrasted by the essential biological role of the ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) enzyme. There are two major forms of catalytically active RuBisCO. Despite a highly conserved active site, the two forms exhibit distinct tertiary structures and sequence heterogeneity. The structure-function relationship between tertiary structure and a proposed trade-off between substrate specificity and catalytic rate is an area of focus in studies to improve RuBisCOs catalytic efficiency. We present results from molecular dynamics simulations of both forms of the activated RuBisCO enzyme. We present results of molecular dynamics simulations of activated form I and II RuBisCO enzymes and identify the inter- and intramolecular interactions that occur through thermal fluctuations.
Sponsoring Department
Colby College. Chemistry Dept.
CLAS Field of Study
Natural Sciences
Event Website
http://www.colby.edu/clas
ID
1061
Tertiary Structure and Active Sites Conformations in Forms I and II RuBisCO
Parker-Reed, SSWAC
A slow catalytic rate and poor substrate discrimination are contrasted by the essential biological role of the ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) enzyme. There are two major forms of catalytically active RuBisCO. Despite a highly conserved active site, the two forms exhibit distinct tertiary structures and sequence heterogeneity. The structure-function relationship between tertiary structure and a proposed trade-off between substrate specificity and catalytic rate is an area of focus in studies to improve RuBisCOs catalytic efficiency. We present results from molecular dynamics simulations of both forms of the activated RuBisCO enzyme. We present results of molecular dynamics simulations of activated form I and II RuBisCO enzymes and identify the inter- and intramolecular interactions that occur through thermal fluctuations.
https://digitalcommons.colby.edu/clas/2015/program/4