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Crystal Structure Determination Of Two New Red Fluorescent Proteins By X-Ray Crystallography
|Title:||Crystal Structure Determination Of Two New Red Fluorescent Proteins By X-Ray Crystallography|
|Keywords:||Red fluorescent protein|
|Date Issued:||Aug 2017|
|Publisher:||University of Hawaiʻi at Mānoa|
|Abstract:||Recently scientists are interested in developing new variants of red fluorescent proteins|
(RFPs), because biosensors basing on RFPs show visual superiority in live-cell imaging. In this
thesis, the structures of two RFP variants, K78BoF and mRuby0.4-3, were investigated by X-ray
crystallography. A monomeric crystal structure of K78BoF was obtained at pH 6 with resolution
at 2.13Å, while a dimeric crystal structure of mRuby0.4-3 was determined at pH 8.2 with
resolution at 2.63Å. Both of their chromophores are formed by Met-Tyr-Gly with K78BoF in the
cis state and mRuby0.4-3 in trans. Hydrogen bonds connecting water molecules and residues to
K78BoF chromophore probably stabilize the conformation of the chromophore and contribute to
the red fluorescence emitted. However, the substitution of an unnatural amino acid pboronophenylalanine
breaks two hydrogen bonds, causing a deviation of the conformation.
Analysis of hydrogen bonds on mRuby0.4-3 chromophore was limited by the relatively low
resolution of the crystal.
|Description:||Ph.D. Thesis. University of Hawaiʻi at Mānoa 2017.|
|Rights:||All UHM dissertations and theses are protected by copyright. They may be viewed from this source for any purpose, but reproduction or distribution in any format is prohibited without written permission from the copyright owner.|
|Appears in Collections:||
Ph.D. - Chemistry|
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