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          <dc:identifier>https://hdl.handle.net/2286/R.I.14732</dc:identifier>
                  <dc:rights>http://rightsstatements.org/vocab/InC/1.0/</dc:rights>
          <dc:rights>All Rights Reserved</dc:rights>
                  <dc:date>2012</dc:date>
                  <dc:format>ix, 118 p. : ill. (chiefly col.)</dc:format>
                  <dc:type>Doctoral Dissertation</dc:type>
          <dc:type>Academic theses</dc:type>
          <dc:type>Text</dc:type>
                  <dc:language>eng</dc:language>
                  <dc:contributor>Kim, Hanseong</dc:contributor>
          <dc:contributor>Wachter, Rebekka M.</dc:contributor>
          <dc:contributor>Fromme, Petra</dc:contributor>
          <dc:contributor>Redding, Kevin E</dc:contributor>
          <dc:contributor>Arizona State University</dc:contributor>
                  <dc:description>Partial requirement for: Ph.D., Arizona State University, 2012</dc:description>
          <dc:description>Includes bibliographical references (p. 108-118)</dc:description>
          <dc:description>Field of study: Chemistry</dc:description>
          <dc:description>The green fluorescent protein (GFP)-like fluorescent proteins play an important role for the color of reef-building corals. Different colors of extant coral fluorescent proteins (FPs) have evolved from a green ancestral protein. Interestingly, green-to-red photoconversion FPs (Kaede-type Red FPs) are only found in clade D from Scleractinia (Faviina suborder). Therefore, I focus on the evolution of Kaede-type FPs from Faviina suborder ancestral FP. A total of 13 mutations have been identified previously that recapitulate the evolution of Kaede-type red FPs from the ancestral green FP. To examine the effect of each mutation, total ten reconstructed FPs were analyzed and six x-ray crystal structures were solved. These substitutions created a more hydrophilic environment around the carbonyl group of Phe61. Also, they increased the flexibility of the c-terminal chain, which keeps it from interacting with the entrance of the putative solvent channel. The photoconversion reaction shows a twophase kinetics. After the rapid initial phase, the overall reaction followed the firstorder kinetics. Based on the crystal structure analysis, I propose a new mechanism for Kaede-type FP photoconversion process, which a proton transfers via Gln38 to the carbonyl group of Phe61.</dc:description>
                  <dc:subject>Biochemistry</dc:subject>
          <dc:subject>Chemistry</dc:subject>
          <dc:subject>Fluorescent Protein</dc:subject>
          <dc:subject>GFP</dc:subject>
          <dc:subject>Kaede</dc:subject>
          <dc:subject>Photoconversion</dc:subject>
          <dc:subject>Fluorescent polymers--Analysis.</dc:subject>
          <dc:subject>Fluorescent polymers</dc:subject>
          <dc:subject>Proteins--Analysis.</dc:subject>
          <dc:subject>Corals--Physiology.</dc:subject>
          <dc:subject>Corals</dc:subject>
                  <dc:title>Color evolution of Kaede-type red fluorescent proteins</dc:title></oai_dc:dc></metadata></record></GetRecord></OAI-PMH>
