IGEM:MIT/2005/IGEM2005: Front Page Summary: Difference between revisions
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<font face="arial narrow" size=5>Members</font> | <font face="arial narrow" size=5>Members</font> | ||
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Image:Ray.jpg|Ray Khan | Image:Ray.jpg|Ray Khan | ||
Image:Jenn.jpg|Jenn Mitchel | Image:Jenn.jpg|Jenn Mitchel | ||
Image:Jenny.jpg|Jenny Nguyen | Image:Jenny beach.jpg|Jenny Nguyen | ||
Image:Annie. | Image:Annie.jpg|Annie Vo | ||
Image:Maxine.jpg|Maxine Yang | Image:Maxine.jpg|Maxine Yang | ||
Image:Jessica.jpg|Jessica Yu | Image:Jessica.jpg|Jessica Yu | ||
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<font face="arial narrow" size=5>Objective</font> | <font face="arial narrow" size=5>Objective</font><br> | ||
<font face="arial narrow" size=5>System Diagram</font><br> | |||
[[Image:SystemAnimation 102105.ppt|Animation PPT]] | |||
<font face="arial narrow" size=5>Cartoon Diagram</font><Br> | |||
[[Image:Diagram SystemComic.jpg]] | |||
<font face="arial narrow" size=5>References</font> | <font face="arial narrow" size=5>References</font> | ||
<br><font size=1.5> | |||
#'''Koh, J. T. (2002). “Engineering selectivity and discrimination into ligand-receptor interfaces.”''' Chemistry & Biology, 9(1), 17-23.<Br>Analysis of receptor-ligand engineering emphasizes high selectivity and ability to discriminate ligand of reengineered receptor. | |||
#'''Wittrup, K. D., Colby D., Yeung Y., Graff C., Swers J., and Kellogg, B. et al (2004). “Engineering antibody affinity by yeast surface display.”''' Methods in Enzymology, 388, 348-358.<Br>This article describes a new method to improve anti-flourescein scFv affinity by yeast surface display technology. | |||
#'''Huston, J. S., Levinson D., Mudgett-Hunter M., and Tai, M. et al (1988). “Protein engineering of antibody binding sites: recovery of specific activity in an anti-digoxin single-chain fv analogue produced in escherichia coli.”''' Proc. Natl. Acad. Sci. USA, 85(16), 5879-5883.<Br>Experiment with anti-digoxin scFv in E.coli, the authors find a way to its improve specificity. | |||
#'''Bedzyk, W. D., Weidner K. M., Denzin L. K., and Johnson, L. S. et al (1990). “Immunological and structural characterization of a high affinity anti-fluorescein single-chain antibody.”''' Journal of Biological Chemistry, 265(30), 18615-18620.<Br>Study on the general characteristics of high affinity anti-flourescein scFv provides insight into scFv affinity improvement. | |||
#'''Mallender, W. D., Carrero J., Voss Jr. E. W. (1996). “Comparative properties of the single chain antibody and fv derivatives of mab 4-4-20. relationship between interdomain interactions and the high affinity for fluorescein ligand.”''' Journal of Biological Chemistry, 271(10), 5338-5346.<Br>Interactions between domains are examined and their affects on affinity of anti-flourescein scFv is observed. | |||
#'''Denzin, L. K., Voss Jr. E. W. (1992). “Construction, characterization, and mutagenesis of an anti-fluorescein single chain antibody idiotype family.”''' Journal of Biological Chemistry, 267(13), 8925-8931.<Br>The authors provide various characteristics of anti-flourescein scFv through construction and mutation. | |||
#'''Pantaliano, M. W., Bird R., Johnson S., and Asel, E. (1991). “Conformational stability, folding, and ligand-binding affinity of single-chain fv immunoglobulin fragments expressed in escherichia coli.”''' Biochemistry, 30(42), 10117-25.<Br>Stability and affinity of scFv are linked to the length of internal linker. | |||
#'''Reiter, Y., Schuck P., Boyd L. F., and Plaksin, D. (1999). “An antibody single-domain phage display library of a native heavy chain variable region: isolation of functional single-domain vh molecules with a unique interface.”''' Journal of Molecular Biology, 290(3), 685-698.<Br>Phage display library is constructed to select for the best scFv. | |||
#'''Shan, D., Press O. W., Tsu T. T., and Hayden, M. (1999). “Characterization of scfv-ig constructs generated from the anti-cd20 mab 1f5 using linker peptides of varying lengths.”''' Journal of Immunology, 162(11), 6589-6595.<Br>The authors examine the effect of linker lengths on affinity of scFv. | |||
#'''Braun, V. (1997). “Surface signaling: novel transcription initiation mechanism starting from the cell surface.”''' Archives of Microbiology, 167(6), 325-331.<Br>This study of Fec pathway in E.coli identifies the major its major components, proteins, and genes involved. | |||
#'''Yue, W. W., Grizot S., Buchanan S. K. (2003). “Structural evidence for iron-free citrate and ferric citrate binding to the tonb-dependent outer membrane transporter FecA.”''' Journal of Molecular Biology, 332(2), 353-368.<Br>Structural differences of bound and unbound FecA protein is explored. | |||
#'''Harle, C., Kim I., Angerer A., and Braun, V. (1995). “Signal transfer through three compartments: transcription initiation of the escherichia coli ferric citrate transport system from the cell surface.”''' EMBO Journal, 14(7), 1430-1438.<Br>This paper demonstrates that ferric citrate uptake into the periplasm is not required for the induction of transcription of fec genes. | |||
#'''Postle, K. (2002). Enhanced: close before opening.''' Science, 295(5560), 1658-1659.<Br>This short article provides summary and brief comparisons of iron transport pathways in E. coli. | |||
#'''Braun, V., Mahren S., Ogierman M. (2003). “Regulation of the feci-type ecf sigma factor by transmembrane signaling.”''' Current Opinion in Microbiology, 6(2), 173-180.<Br>The authors identifie the components of Fec pathway that are required for signaling. | |||
#'''Ferguson, A. D., Chakraborty R., Smith B. S., and Esser, L. et al (2002). “Structural basis of gating by the outer membrane transporter FecA.”''' Science, 295(5560), 1715-1719.<Br>Crystal structure of FecA protein shows the location of conformational change upon binding to ferric citrate. |
Latest revision as of 11:22, 22 May 2006
http://openwetware.org/images/a/ac/FrontpageBanner_v5.jpg
Members
-
Will Bosworth
-
Ray Khan
-
Jenn Mitchel
-
Jenny Nguyen
-
Annie Vo
-
Maxine Yang
-
Jessica Yu
-
Mascot
Objective
System Diagram
File:SystemAnimation 102105.ppt
Cartoon Diagram
References
- Koh, J. T. (2002). “Engineering selectivity and discrimination into ligand-receptor interfaces.” Chemistry & Biology, 9(1), 17-23.
Analysis of receptor-ligand engineering emphasizes high selectivity and ability to discriminate ligand of reengineered receptor. - Wittrup, K. D., Colby D., Yeung Y., Graff C., Swers J., and Kellogg, B. et al (2004). “Engineering antibody affinity by yeast surface display.” Methods in Enzymology, 388, 348-358.
This article describes a new method to improve anti-flourescein scFv affinity by yeast surface display technology. - Huston, J. S., Levinson D., Mudgett-Hunter M., and Tai, M. et al (1988). “Protein engineering of antibody binding sites: recovery of specific activity in an anti-digoxin single-chain fv analogue produced in escherichia coli.” Proc. Natl. Acad. Sci. USA, 85(16), 5879-5883.
Experiment with anti-digoxin scFv in E.coli, the authors find a way to its improve specificity. - Bedzyk, W. D., Weidner K. M., Denzin L. K., and Johnson, L. S. et al (1990). “Immunological and structural characterization of a high affinity anti-fluorescein single-chain antibody.” Journal of Biological Chemistry, 265(30), 18615-18620.
Study on the general characteristics of high affinity anti-flourescein scFv provides insight into scFv affinity improvement. - Mallender, W. D., Carrero J., Voss Jr. E. W. (1996). “Comparative properties of the single chain antibody and fv derivatives of mab 4-4-20. relationship between interdomain interactions and the high affinity for fluorescein ligand.” Journal of Biological Chemistry, 271(10), 5338-5346.
Interactions between domains are examined and their affects on affinity of anti-flourescein scFv is observed. - Denzin, L. K., Voss Jr. E. W. (1992). “Construction, characterization, and mutagenesis of an anti-fluorescein single chain antibody idiotype family.” Journal of Biological Chemistry, 267(13), 8925-8931.
The authors provide various characteristics of anti-flourescein scFv through construction and mutation. - Pantaliano, M. W., Bird R., Johnson S., and Asel, E. (1991). “Conformational stability, folding, and ligand-binding affinity of single-chain fv immunoglobulin fragments expressed in escherichia coli.” Biochemistry, 30(42), 10117-25.
Stability and affinity of scFv are linked to the length of internal linker. - Reiter, Y., Schuck P., Boyd L. F., and Plaksin, D. (1999). “An antibody single-domain phage display library of a native heavy chain variable region: isolation of functional single-domain vh molecules with a unique interface.” Journal of Molecular Biology, 290(3), 685-698.
Phage display library is constructed to select for the best scFv. - Shan, D., Press O. W., Tsu T. T., and Hayden, M. (1999). “Characterization of scfv-ig constructs generated from the anti-cd20 mab 1f5 using linker peptides of varying lengths.” Journal of Immunology, 162(11), 6589-6595.
The authors examine the effect of linker lengths on affinity of scFv. - Braun, V. (1997). “Surface signaling: novel transcription initiation mechanism starting from the cell surface.” Archives of Microbiology, 167(6), 325-331.
This study of Fec pathway in E.coli identifies the major its major components, proteins, and genes involved. - Yue, W. W., Grizot S., Buchanan S. K. (2003). “Structural evidence for iron-free citrate and ferric citrate binding to the tonb-dependent outer membrane transporter FecA.” Journal of Molecular Biology, 332(2), 353-368.
Structural differences of bound and unbound FecA protein is explored. - Harle, C., Kim I., Angerer A., and Braun, V. (1995). “Signal transfer through three compartments: transcription initiation of the escherichia coli ferric citrate transport system from the cell surface.” EMBO Journal, 14(7), 1430-1438.
This paper demonstrates that ferric citrate uptake into the periplasm is not required for the induction of transcription of fec genes. - Postle, K. (2002). Enhanced: close before opening. Science, 295(5560), 1658-1659.
This short article provides summary and brief comparisons of iron transport pathways in E. coli. - Braun, V., Mahren S., Ogierman M. (2003). “Regulation of the feci-type ecf sigma factor by transmembrane signaling.” Current Opinion in Microbiology, 6(2), 173-180.
The authors identifie the components of Fec pathway that are required for signaling. - Ferguson, A. D., Chakraborty R., Smith B. S., and Esser, L. et al (2002). “Structural basis of gating by the outer membrane transporter FecA.” Science, 295(5560), 1715-1719.
Crystal structure of FecA protein shows the location of conformational change upon binding to ferric citrate.