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Determination of Telomeric Protein Interaction Binding Sites Between Amino Acids 58-268 of TRF1 and 224-276 of TIN2 and Between Amino Acids 42-245 of TRF2 and 203-361 of TIN2

dc.contributor.advisorLei, Ming
dc.contributor.authorAnstett, Danielle
dc.date.accessioned2008-03-14T13:30:47Z
dc.date.available2008-03-14T13:30:47Z
dc.date.copyright2006-04-28
dc.date.issued2006-04-28
dc.identifier.urihttp://hdl.handle.net/10920/4433
dc.description1 broadside : ill.
dc.description.abstractTelomerase: • A ribonucleoprotein complex, with RNA and protein components, in all eukaryotes • Required for lengthening the ends of telomeric DNA by reverse transcriptase Without Telomerase: • Unable to lengthen chromosomes, DNA shortens with each replication • Results in the loss of genetic information and greater susceptibility to mutation Unknown: • The exact amino acid interactions of the telomeric proteins • The nature of the interaction between certain telomeric proteins The Study will: • Examine the relations of three telomeric proteins, TRF1, TRF2, and TIN2 • Attempt to form complexes with protein fragments of decreasing size (Figure 1) • Examine the interaction between TRF1 and TRF2 • Lead to greater understanding concerning telomeric protein bindingen
dc.description.sponsorshipUniversity of Michigan.
dc.description.tableofcontentsIntroduction -- Methods -- Results -- Discussion -- Literature -- Acknowledgments
dc.language.isoen_USen
dc.publisherKalamazoo College
dc.subject.lcshAmino acids
dc.subject.lcshDNA
dc.titleDetermination of Telomeric Protein Interaction Binding Sites Between Amino Acids 58-268 of TRF1 and 224-276 of TIN2 and Between Amino Acids 42-245 of TRF2 and 203-361 of TIN2en
dc.typePresentationen


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  • Diebold Symposium Posters and Schedules [479]
    Poster and oral presentations by senior biology majors that include the results of their Senior Integrated Projects (SIPs) at the Diebold Symposium. Abstracts are generally available to the public, but PDF files are available only to current Kalamazoo College students, faculty, and staff.

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