Endogenous and chemical modifications of model proteins

Protein modifications are ubiquitous in nature, introducing biological complexity and functional diversity. Of the known post-translational modifications, glycosylation is one of the most common and most complex, yet some of the biological implications of this modification remain poorly understood. The development of chemical tools to mimic these modifications is helping to elucidate their biological roles and improve the range of biopharmaceuticals. To probe the biochemistry of endogenous glycosylation and to test the efficacy of novel synthetic modifications, tractable protein scaffolds are needed. Previously, members of the pancreatic-type ribonuclease (ptRNases) superfamily have been utilized as model protein scaffolds. They are a class of highly conserved, secretory endoribonucleases that mediate diverse biological functions through the cleavage of RNA.

Name thesis:degree_name

Doctoral

Department dc:contributor.department

Massachusetts Institute of Technology. Department of Chemistry

Grantor dc:publisher

Massachusetts Institute of Technology

Year dc:date.issued

2019

Author dc:creator

• Ressler, Valerie T.(Valerie Terynn)

Advisor dc:contributor.advisor

• Ronald T. Raines.

• Chemistry.

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/1721.1/121784

OAI identifier oai:identifier

oai:dspace.mit.edu:1721.1/121784