Predicting self-assembly in globular protein-polymer bioconjugates

Globular proteins offer powerful solutions for addressing challenges in the fields of medicine, industry, defense, and energy. Enzymes perform reactions with high efficiency and specificity, allowing for minimal generation of undesired side products even while exhibiting rapid turnover-traits difficult to replicate in synthetic catalysts. These targets make proteins attractive tools for immobilization to form functional catalysts and sensors. Nevertheless, there are many challenges in creating these advanced materials. The activity of the protein must be retained, and control over the structure of the material is desirable. Protein-polymer block copolymers offer an attractive solution to these issues. These materials have been shown to selfassemble into ordered nanodomains while retaining protein activity. However, the phase behavior of these materials is not fully understood due to the complex nature of anisotropic interactions between the proteins.

Name thesis:degree_name

Doctoral

Department dc:contributor.department

Massachusetts Institute of Technology. Department of Chemical Engineering

Grantor dc:publisher

Massachusetts Institute of Technology

Year dc:date.issued

2018

Author dc:creator

• Huang, Aaron.

Advisor dc:contributor.advisor

• Bradley D. Olsen.

• Chemical Engineering.

Statement dc:rights

• MIT theses are protected by copyright. They may be viewed, downloaded, or printed from this source but further reproduction or distribution in any format is prohibited without written permission.

Licence dc:rights.uri

• http://dspace.mit.edu/handle/1721.1/7582

Language dc:language.iso

eng

Handle dc:identifier.uri

https://hdl.handle.net/1721.1/121893

OAI identifier oai:identifier

oai:dspace.mit.edu:1721.1/121893