Mechanistic studies of photochemical protein modification using 1,8-naphthalimides.

Simple item page
dc.contributor.advisorKane, Robert R.
dc.contributor.authorKang, Ae Gyeong.
dc.contributor.departmentChemistry and Biochemistry.en
dc.contributor.otherBaylor University. Dept. of Chemistry and Biochemistry.en
dc.date.accessioned2009-08-25T16:07:41Z
dc.date.available2009-08-25T16:07:41Z
dc.date.copyright2009-08
dc.date.issued2009-08-25T16:07:41Z
dc.descriptionIncludes bibliographical references (p. 60-63).en
dc.description.abstractCertain 4-alkylamino-1,8-naphthalimides have been used as photosensitizers for photochemical protein crosslinking. In my research various types of 4-amino and N-substituents naphthalimides have been synthesized and studied for application to protein crosslinking and tissue bonding. Ribonuclease A (RNase A) was used as a model protein in the protein for crosslinking studies. The photochemical crosslinking experiments were analyzed using SDS-PAGE electrophoresis and western blot detection. Biotinylated naphthalimides were also synthesized and it was demonstrated that while they could catalyze photochemical protein crosslinking, they were not incorporated into the crosslinked proteins. It was shown previously that tyrosine and histidine residues were involved in protein crosslinking through type I and type II mechanisms. Therefore, suspect amino acids such as tyramine, tryptamine, L-tryptophan, and dopamine were combined with biotin in order to allow us to detect their incorporation into the photooxidized protein. It was also shown that the biotin-tyramine compound and biotin-LC-hydrazide can serve as inhibitors of photochemical protein crosslinking. These studies serve to allow us to better understand mechanism of photochemical protein crosslinking.en
dc.description.degreeM.S.en
dc.description.statementofresponsibilityby Ae Gyeong Kang.en
dc.format.extentix, 63 p. : ill.en
dc.format.extent59801 bytes
dc.format.extent1830111 bytes
dc.format.mimetypeapplication/pdf
dc.format.mimetypeapplication/pdf
dc.identifier.urihttp://hdl.handle.net/2104/5383
dc.language.isoen_USen
dc.rightsBaylor University theses are protected by copyright. They may be viewed from this source for any purpose, but reproduction or distribution in any format is prohibited without written permission. Contact librarywebmaster@baylor.edu for inquiries about permission.en
dc.rights.accessrightsWorldwide accessen
dc.subjectProteins -- Crosslinking.en
dc.subjectPhotochemistry.en
dc.subjectBiomechanics.en
dc.titleMechanistic studies of photochemical protein modification using 1,8-naphthalimides.en
dc.typeThesisen

Files

Original bundle

Now showing 1 - 2 of 2
Thumbnail Image
Name:
AeGyeong_Kang_masters.pdf
Size:
1.75 MB
Format:
Adobe Portable Document Format
Description:
Thesis
Download
No Thumbnail Available
Name:
AeGyeong_Kang_permissions.pdf
Size:
58.4 KB
Format:
Adobe Portable Document Format
Description:
Permissions Form
Download

License bundle

Now showing 1 - 1 of 1
No Thumbnail Available
Name:
license.txt
Size:
1.95 KB
Format:
Item-specific license agreed upon to submission
Description:
Download

Collections

Electronic Theses and Dissertations