Francis Lab

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Welcome to the Francis lab wiki!  Please visit our [http://www.cchem.berkeley.edu/francisgrp/ website].
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Welcome to the Francis lab wiki!  Please visit our [http://wasabi.cchem.berkeley.edu website].
== Lab Information ==
== Lab Information ==
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We're just getting started here - bare with us as we update our information soon!
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The Francis group is interested in the design of new materials by protein modification. In order to tackle a large engineering project on proteins, and in particular designing in multiple orthogonal functions onto a single scaffold, the group also devotes a great deal of it's effort toward the creation of new site-selective protein modifications. Our work then focuses on two areas of development: Methodology and Materials.
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==Methodology==
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Our methodology work primarily targets native amino acid residues. Thusfar, we have developed new native modifications of Tyrosine, by alkylation and a Mannich-Type coupling, Tryptophan, by using rhodium carbenoids, the N-Terminus of proteins, and amines, by reductive amination.
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==Materials==
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Our groups Materials projects employ existing and new modifications of protein sidechains as a means of building up scaffolds for projects that require, or benefit from, site-selective, spatially arranged function. Our work has shown that intact viral capsids can be transferred to organic solvent, and that the spherical viral capsid MS2 can possibly be used as a drug delivery unit.

Current revision

Welcome to the Francis lab wiki! Please visit our website.

Lab Information

The Francis group is interested in the design of new materials by protein modification. In order to tackle a large engineering project on proteins, and in particular designing in multiple orthogonal functions onto a single scaffold, the group also devotes a great deal of it's effort toward the creation of new site-selective protein modifications. Our work then focuses on two areas of development: Methodology and Materials.

Methodology

Our methodology work primarily targets native amino acid residues. Thusfar, we have developed new native modifications of Tyrosine, by alkylation and a Mannich-Type coupling, Tryptophan, by using rhodium carbenoids, the N-Terminus of proteins, and amines, by reductive amination.


Materials

Our groups Materials projects employ existing and new modifications of protein sidechains as a means of building up scaffolds for projects that require, or benefit from, site-selective, spatially arranged function. Our work has shown that intact viral capsids can be transferred to organic solvent, and that the spherical viral capsid MS2 can possibly be used as a drug delivery unit.

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