Publication Date
2015
Document Type
Dissertation/Thesis
First Advisor
Horn, James R.
Degree Name
Ph.D. (Doctor of Philosophy)
Legacy Department
Department of Chemistry and Biochemistry
LCSH
Biochemistry; Biophysics; Molecular biology; Antigen-antibody reactions; Thermodynamics; Immunoglobulins; Chemistry; Analytic--Technique
Abstract
Antibody fragments are attractive alternatives to conventional antibodies for both therapeutic and diagnostic applications. One example, single-domain VHH antibodies, which are derived from camelid heavy chain-only antibodies, display comparable binding affinity to conventional antibodies despite the significantly reduced binding interface. Here, an anti-RNase A VHH single-domain antibody and its antigen, RNase A, are used as a model antibody-antigen system for the three studies described in this dissertation.
Recommended Citation
Jakkaraju, Sriram, "The thermodynamic dissection and design of high-affinity antibodies" (2015). Graduate Research Theses & Dissertations. 6347.
https://huskiecommons.lib.niu.edu/allgraduate-thesesdissertations/6347
Extent
165 pages
Language
eng
Publisher
Northern Illinois University
Rights Statement
In Copyright
Rights Statement 2
NIU theses are protected by copyright. They may be viewed from Huskie Commons for any purpose, but reproduction or distribution in any format is prohibited without the written permission of the authors.
Media Type
Text
Comments
Advisors: James R. Horn.||Committee members: Gary Baker; Timothy Hagen; Victor Ryzhov; Yanbin Yin.