Large scale motions in a biosensor protein glucose oxidase: A combined approach by QENS, normal mode analysis, and molecular dynamics studies

Document Type

Article

Publication Date

7-1-2008

Department

Mechanical Engineering

Abstract

The characteristics of the glucose oxidase were studied using a combination of experimental and theoretical techniques. Quasi elastic neutron scattering experiments were used to obtain the vibrational frequencies of the protein. These were compared to theoretical results obtained by normal mode analysis. Results indicate a good match between the experimental and theoretical values. Molecular dynamic simulation with covariant analysis was used to study the structure and dynamics of glucose oxidase. Various parameters like the radius of gyration, root mean square fluctuations, solvent accessibility were studied for evaluating the structural stability of the protein. The frequency of vibration calculated from the three methods is used to derive the large scale motions. Theses studies were used to predict the suitable lysine residues for linkage with carbon nanotubes. © 2008 Wiley Periodicals, Inc.

DOI

10.1002/bip.20956

First Page

582

Last Page

594

Publication Title

Biopolymers

Comments

At the time of publication, Richard T. Schoephoerster was affiliated with Florida International University.

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