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Investigation of talin head-tail interactions
- Date Issued:
- 2009
- Summary:
- Talin is a ubiquitous, high-molecular-weight, flexible protein that plays a critical role in focal adhesions by activating, as well as connecting, integrins to the actin cytoskeleton. Talin's inactive auto-inhibitory state is speculated to be one of its modes of regulation inside the cell and is achieved through its head-tail interactions. In order to decipher the stability of this interaction, the head domain (residues 206-405) was cloned into a modified pET28m vector while the tail domains (residues 1654-2344 and 2225-2344) were cloned into the pET32a vector to obtain octa-histidine tagged and un-tagged peptide, respectively. Neither co-expression nor pull-down using the His-tagged head domain was successful in purifying a stable head-tail complex. Our results indicate rather weak interactions between the talin head and rod domains and hence, under our experimental conditions, do not lead to a stable auto-inhibitory complex that can be purified for further studies.
Title: | Investigation of talin head-tail interactions. |
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Name(s): |
Butyn, Amber. Harriet L. Wilkes Honors College |
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Type of Resource: | text | |
Genre: | Thesis | |
Issuance: | multipart monograph | |
Date Issued: | 2009 | |
Publisher: | Florida Atlantic University | |
Physical Form: |
electronic electronic resource |
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Extent: | vi, 35 leaves : ill. (some col.) ; 29 cm. | |
Language(s): | English | |
Summary: | Talin is a ubiquitous, high-molecular-weight, flexible protein that plays a critical role in focal adhesions by activating, as well as connecting, integrins to the actin cytoskeleton. Talin's inactive auto-inhibitory state is speculated to be one of its modes of regulation inside the cell and is achieved through its head-tail interactions. In order to decipher the stability of this interaction, the head domain (residues 206-405) was cloned into a modified pET28m vector while the tail domains (residues 1654-2344 and 2225-2344) were cloned into the pET32a vector to obtain octa-histidine tagged and un-tagged peptide, respectively. Neither co-expression nor pull-down using the His-tagged head domain was successful in purifying a stable head-tail complex. Our results indicate rather weak interactions between the talin head and rod domains and hence, under our experimental conditions, do not lead to a stable auto-inhibitory complex that can be purified for further studies. | |
Identifier: | 459787318 (oclc), 209984 (digitool), FADT209984 (IID), fau:1358 (fedora) | |
Note(s): |
by Amber Butyn. Thesis (B.A.)--Florida Atlantic University, Honors College, 2009. Bibliography: leaves 32-35. Electronic reproduction. Boca Raton, Fla., 2009. Mode of access: World Wide Web. |
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Subject(s): |
Membrane proteins -- Structure-activity relationships Cell membranes -- Physiology Molecular biology Cell interaction Developmental cytology |
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Held by: | FBoU FAUER | |
Persistent Link to This Record: | http://purl.flvc.org/FAU/209984 | |
Use and Reproduction: | Copyright © is held by the author, with permission granted to Florida Atlantic University to digitize, archive and distribute this item for non-profit research and educational purposes. Any reuse of this item in excess of fair use or other copyright exemptions requires permission of the copyright holder. | |
Host Institution: | FAU |