Modification of maltose binding protein for generation of nanomaterials and for improving crystallization
Authors
Srinivasan, Usha
ORCID
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Other Contributors
Breneman, Curt M.
Bell, Jeffrey
Wentland, Mark P.
Colón, Wilfredo
Bell, Jeffrey
Wentland, Mark P.
Colón, Wilfredo
Issue Date
2001-08
Keywords
Chemistry
Degree
PhD
Terms of Use
This electronic version is a licensed copy owned by Rensselaer Polytechnic Institute, Troy, NY. Copyright of original work retained by author.
Full Citation
Abstract
Protein crystallization can be considered as a self-assembly process, since protein molecules in solution form a well-ordered lattice in the crystal. Self-assembly processes are a common route to generating nanomaterials. Nanomaterials can be generated from protein crystals by crosslinking the adjacent molecules in the protein crystal. By engineering cysteine mutations on the surface of the protein of interest, such that crystallization brings the cysteine residues close enough to form disulfide bonds, adjacent molecules in the crystal can be covalently crosslinked. Based on the position and number of crosslinks, different nanoarchitectures such as protein fibers and sheets can be generated. This strategy was applied to maltose binding protein (MBP) and crosslinked crystals of MBP were obtained. Fibers of MBP were obtained on dissociation of the crystals.
Description
August 2001
School of Science
School of Science
Department
Dept. of Chemistry
Publisher
Rensselaer Polytechnic Institute, Troy, NY
Relationships
Rensselaer Theses and Dissertations Online Collection
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