Computational analysis of the phylogeny and thermodynamics of glycoside hydrolases
Date
Authors
Major Professor
Advisor
Committee Member
Journal Title
Journal ISSN
Volume Title
Publisher
Altmetrics
Authors
Research Projects
Organizational Units
The function of the Department of Chemical and Biological Engineering has been to prepare students for the study and application of chemistry in industry. This focus has included preparation for employment in various industries as well as the development, design, and operation of equipment and processes within industry.Through the CBE Department, Iowa State University is nationally recognized for its initiatives in bioinformatics, biomaterials, bioproducts, metabolic/tissue engineering, multiphase computational fluid dynamics, advanced polymeric materials and nanostructured materials.
History
The Department of Chemical Engineering was founded in 1913 under the Department of Physics and Illuminating Engineering. From 1915 to 1931 it was jointly administered by the Divisions of Industrial Science and Engineering, and from 1931 onward it has been under the Division/College of Engineering. In 1928 it merged with Mining Engineering, and from 1973–1979 it merged with Nuclear Engineering. It became Chemical and Biological Engineering in 2005.
Dates of Existence
1913 - present
Historical Names
- Department of Chemical Engineering (1913–1928)
- Department of Chemical and Mining Engineering (1928–1957)
- Department of Chemical Engineering (1957–1973, 1979–2005)
- Department of Chemical and Biological Engineering (2005–present)
- College of Engineering(parent college)
Related Units
Journal Issue
Is Version Of
Versions
Series
Department
Abstract
My research has focused on using computation by means of phylogenetic analysis and molecular mechanics docking studies to further extend knowledge of glycoside hydrolases (GHs). Phylogenetic analysis was used to crystallize the fundamental differences between specific types of cellulases in GH family 6 (GH6). Cellulase enzymes were then examined for functional divergence in order to determine the cause of substrate specificity, finding that very often, active site amino acid residues were highly retained, but surface residues had changed over time, most likely to help interact with other enzymes or larger substrates. Automated docking was able to provide support for the existence of several putative subsites within GH6 enzymes, along with providing more information about the possible residues to play the role of catalytic base.