dc.contributor.author	Hill, Willie Darrell, Jr.
dc.date.accessioned	2022-08-29T19:53:30Z
dc.date.available	2022-08-29T19:53:30Z
dc.date.issued	2022-07
dc.identifier.other	EA5F4695-00A5-CE97-4824-CC723BE38B43	en_US
dc.identifier.uri	https://hdl.handle.net/10428/5879
dc.description.abstract	Albumin is one of the most studied proteins because of its diverse functions (Peters, 1995). Albumin varies between species, but past research on Human Serum Albumin (HSA) and Bovine Serum Albumin (BSA) has shown structural similarities between the two. Binding properties of HSA and BSA can be compared using the thermodynamic parameters of enthalpy, entropy, and Gibbs free energy (ΔH, ΔS, and ΔG). Previous studies have shown a linear relationship between enthalpy and entropy when temperature is held constant (enthalpy-entropy compensation). Prior data used thermodynamics to compare the two proteins on a micro-level (1-10 ligands). This thesis is the first to statistically analyze thermodynamic quantities in the binding of ligands to HSA and BSA on a macro-level (200+ ligands). A bioinformatic approach was used to obtain thermodynamic data from 197 primary literature sources available in PubMed (Sayer, et al., 2022). Linear regression was applied and showed a significant positive correlation between enthalpy and entropy in both proteins examined. The findings indicate the existence of a significant enthalpy-entropy compensation. This thesis quantitatively described the variation of ΔH°, ΔS°, ΔG° in the binding of ligands to BSA and HSA by using Cumulative Distribution Function (CDF). The obtained CDFs were used to derived Normalized Probability Density Function (NPDF) for each thermodynamic quality. The Shannon entropy was calculated to assess the variability on ΔH°, ΔS°, ΔG°. The resulting values of Shannon entropy shows that both ΔH° and TΔS° have larger values than that of ΔG° for both proteins. ΔG° contained lower levels of information (uncertainty) than ΔH° and TΔS° for both proteins. Keywords: Bovine Serum Albumin; Human Serum Albumin; Thermodynamics; Enthalpy; Entropy;	en_US
dc.description.tableofcontents	-- Data collection 6 -- Linear regression analysis of ΔH° and ΔS° 6 -- Cumulative distributions of ΔH°, TΔS°, and ΔG° 6 -- Normalized Probability distribution function of ΔH°, TΔS°, and ΔG° 7 -- Venn diagrams for ΔH°, TΔS°, and ΔG° of BSA and HSA 7 -- Shannon entropy for NDPF of ΔH°, TΔS°, and ΔG° 8 -- Mathematical software 8 -- Chapter III: RESULTS 9 -- Enthalpy–entropy compensation 9 -- Cumulative distribution of thermodynamic quantities 12 -- Normalized probability density distributions of thermodynamic quantities 12 -- Shannon entropy of ΔH°, TΔS°, and ΔG° 19 -- Chapter IV : DISCUSSION 23 -- REFERENCES 25 -- APPENDIX A: ΔH° and ΔS° for BSA and HSA binding to different ligands 29	en_US
dc.format.extent	1 electronic document and derivatives, 44 pages. 932719 bytes.	en_US
dc.format.mimetype	application/pdf	en_US
dc.language.iso	en_US	en_US
dc.rights	This dissertation is protected by the Copyright Laws of the United States (Public Law 94-553, revised in 1976). Consistent with fair use as defined in the Copyright Laws, brief quotations from this material are allowed with proper acknowledgement. Use of the materials for financial gain with the author's expressed written permissions is not allowed.	en_US
dc.subject	Academic theses	en_US
dc.subject	Biology	en_US
dc.subject	Enthalpy	en_US
dc.subject	Entropy	en_US
dc.subject	Thermodynamics	en_US
dc.title	Statistical Analysis of Thermodynamic Quantities in the Binding of Ligands to Bovine and Human Serum Albumin	en_US
dc.type	Thesis	en_US
dc.contributor.department	Department of Biology of the College of Science and Mathematics	en_US
dc.description.advisor	Kang, Jonghoon
dc.description.committee	Blackmore, Mark
dc.description.committee	James, Christine
dc.description.degree	M.S.	en_US
dc.description.major	Biology	en_US