Jonathan A. King
Prof., Molecular Biology


Updated: April 2014


Yale University, New Haven, CT.




Caltech, Pasadena, CA




British Medical Research Council,
Cambridge, England

Postdoc Fellow


Structural Biology


Associate Scientist, Jet Propulsion Laboratory, Pasadena CA,


Assistant Professor, Department of Biology, M.I.T.


Associate Professor, Department of Biology, M.I.T.


Director of Biomedical Electron Microscopy Lab., M.I.T.


Professor, Department of Biology, M.I.T.



General Motors National Scholar


B.S.magna cum laude
High Honors in Zoology, Yale


Woodrow Wilson National Fellow


Jane Coffin Childs Fund Fellow


U.S. Antarctic Service Medal


Foundation Lecturer, ASM


Fellow, AAAS


Guggenheim Fellow


NIH Merit Award


President, Biophysical Society 1999
MIT Martin Luther King Leadership Award 2003
Distinguished Biology Award, 9th Annual International RECOMB Conference 2005

Professional Services
Chair, Massachusetts Darwin Bicentennial Project 2008-present
Massachusetts Academy of Sciences, Board of Trustees 2008-present
NEI Board of Scientific Counselors 2005-08
Chair, XVIII International Conference on Phage/Virus Assembly 2003

Executive Board Member, Biophysical Society


Joint Steering Committee for Public Policy Board Member


Technical Education Resource Center Board of Trustees


National Councillor, Biophysical Society


FASEB Summer Research Conferences Advisory Committee


Chair, Gordon Conference on Proteins


Councillor, Am. Soc. Virology


NIH Genetic Basis of Disease Study Section


NIH Biotechnology Training Grant Study Section


NIH Structural Biology Study Section


Chair, FASEB Virus Assembly Conference


Co-Chair, FASEB In Vivo Protein Folding Conf.


Chair, AAAS Meeting on Protein Folding


Editorial Board, Annual Reviews of Microbiology


NIH Microbial Physiology Study Section


Committee on Nominations, American Association for the Advancement of Science


Chair, Bacterial Virus Division, American Society of Microbiology



Publications: Jonathan King; 1988-2014

Total Number of Publications: 249

78. Yu M-H and King J. Surface Amino Acids as Sites of Temperature-Sensitive Folding Mutations in the P22 Tailspike Protein. (1988) J. Biol. Chem. 263(3), 1424-1431.

79. Sargent D, Benevides JM, Yu M-H, King J and Thomas GJ Jr. (1988) Secondary Structure and Thermostability of the Phage P22 Tailspike: Analysis of Raman Spectroscopy of the Wild-Type Protein and a Temperature-Sensitive Folding Mutant. J. Mol. Biol. 199(3), 491-502.

80. King, J. and Haase-Pettingell, C. (1988) Aggregate Formation from a Thermolabile Intermediate in the Maturation of the Thermostable P22 Tailspike Protein. In British Biochem. Society Transactions. 16(2), 105-108.

81. Bazinet C, Benbaset J, King J, Carazo J and Carrascosa J. (1988) Purification and Organization of the Gene 1 Portal Protein Required for Phage P22 DNA Packaging. Biochem. 27, 1849-1856.

82. Haase-Pettingell C and King J. (1988) Formation aggregates from a thermolabile in vivo intermediate in P22 tailspike maturation. A model for inclusion body formation. J. Biol. Chem. 263(10), 4977-4983.

83. Bazinet C, and King J. (1988) Initiation of P22 Procapsid Assembly in vivo. J. Mol. Biol. 202, 77-86.

84. Prevelige PE Jr, Thomas D and King J. (1988) Scaffolding Protein Regulates the Polymerization of P22 Coat Subunits into Icosahedral Shells in vivo. J. Mol. Biol. 202, 743-757.

85. Villafane R and King J. (1988) Nature and Distribution of Sites of Temperature Sensitive Folding Mutations in the Gene for the P22 Tailspike Polypeptide Chain. J. Mol. Biol., 204, 607 - 619.

86. Mitraki A and King J. (1989) "Protein folding intermediates and inclusion body formation." Bio/technology, 7, 690 - 697.

87. Sturtevant J, Yu M-H, Haase-Pettingell C and King J. (1989) Thermostability of temperature-sensitive folding mutants of the P22 tailspike protein. J. Biol. Chem. 264(18), 10693-10698.

88. King J. (1989) Deciphering the rules of protein folding. Chem. & Eng. News, April 11, 32-54. No abstract available.

89. Seckler R, Fuchs A, King J and Jaenicke R. (1989) Reconstitution of the thermostable trimeric phage P22 tailspike protein from denatured chains in vitro. J. Biol. Chem., 264, 11750 - 11753.

90. King, J., Fane, B., Haase-Pettingell, C., Mitraki, A., Villafane, R., and Yu, M-H. (1989) "Identification of amino acid sequences influencing intracellular folding pathways using temperature sensitive folding mutations." In "Protein Folding: Deciphering the Second Half of the Genetic Code" (L. A. Gierasch and J. King, eds.) AAAS, pp 225-240.

91. King, J., Fane, B., Haase-Pettingell, C., Mitraki, A. and Villafane, R. (1990) "Genetic analysis of polypeptide chain folding and misfolding" in vivo. In, "Protein Design and the Development of New Therapeutics and Vaccines." (Ed. Jerry Hook &;George Poste) Smith Kline and French Symposium, Plenum Press, 59-78.

92. Thomas GJ Jr, Becka R, Sargent D, Yu M-H and King J. (1990) Conformational stability of P22 Tailspike Proteins Carrying Temperature Sensitive Folding Mutations.Biochem., 29, 4181-4187.

93. Prevelige PE Jr, Thomas,D, King J, Towse SA, and Thomas G J Jr. (1990) Conformational states of the bacteriophage P22 capsid subunit in relation to self-assembly. Biochem., 29, 5626-5633.

94. Friguet B, Djavadi-Ohaniance L, Haase-Pettingell C, King J, and Goldberg M. (1990) Properties of monoclonal antibodies selected for probing the conformation of wild type and mutant forms of the P22 tailspike endorhamnosidase. J. Biol. Chem., 265(18), 10347-10351.

95. Gierasch LA and King J. Protein Folding: Deciphering the Second Half of the Genetic Code (1990) American Association for the Advancement of Science, Wash. D.C.

96. Bazinet C, Villafane R and King J. (1990) Novel second-site suppression of cold-sensitive defect in phage P22 procapsid assembly.J. Mol. Biol. 216, 701-716.

97. Fane B and King J. (1991) Intragenic suppressors of folding defects in the P22 tailspike protein. Genetics 127: 263-277.

98. Chen B and King J. (1991) Thermal unfolding pathway for the thermostable P22 tailspike endorhamnosidase.Biochemistry, 30, 6260-6269.

99<. Fane B, Villafane R, Mitraki A, and King J. (1991) Identification of global suppressors for temperature-sensitive folding mutants of the P22 tailspike protein. J. Biol. Chem. 266(18), 11640-11648.

100. Mitraki A, Fane B, Haase-Pettingell C, Sturtevant J and King J. (1991) Global suppression of protein folding defects and inclusion body formation. Science, 253, 54-58.

101. Chen, B. and King, J. (1991) "Pathway for the thermal unfolding of wild type and mutant forms of the thermostable P22 tailspike endorhamnosidase." In "Protein Refolding" (G. Georgiou &;E. de Bernardez Clark, eds.) ACS Symposium Series 470, American Chemical Society, Washington, D.C., pp. 119-132.

102. Mitraki, A., Haase-Pettingell, C., and King J. (1991) "Mechanisms of inclusion body formation." In "Protein Refolding" (G. Georgiou & E. de Bernardez-Clark, eds.) ACS Sympsosium Seris 470, American Chemical Society, Washington, D.C., pp. 35-49.

103. Mitraki, A., Fane, B., Haase-Pettingell, C. and King, J. (1991) "Mutations affecting protein folding and misfolding in vivo." In "Application in Enzyme Biotechnology" (eds. T. Baldwin and J. Kelly) Plenum Press, pp. 129-136.

104. Chen C-C, Zhu Y, King J and Evans L. (1992) A Molecular Thermodynamic Approach to Predict the Secondary structure of Homo-polypeptides in Aqueous Systems.Biopolymers, 32, 1375-1392.

105. Mitraki A and King J. (1992) Amino acid substitutions influencing intracellular protein folding pathways. FEBS Letters, 307(1), 20-25.

106. Teschke C and King J. (1992) Folding and assembly of oligomeric proteins in Escherichia coli. Current Opinion in Biotechnology, 3(5), 468-473.

107. Zhu Y, Chen C-C, King J and Evans L. (1992) Molecular Thermodynamic Model To Predict the α-Helical Secondary Structure of Polypeptide Chains in Solution." Biochemistry, 31, 10591-10601.

108. Prevelige P, Thomas D and King J. (1993) Nucleation and Growth Phases in the Polymerization of Coat and Scaffolding Subunits into Icosahedral Procapsid Shells. Biophysical Journal, 64, 824-835.

109. King J, Haase-Pettingell C, Gordon C, Sather S and Mitraki A. (1993) Amino Acid Sequence Determinants of Polypeptide Chain Folding and Inclusion Body Formation. In "Protein Folding: In Vivo and In Vitro" (ed. J. Cleland) ACS Symposium Series 526, American Chemical Society, Washington, D.C., pp. 24-37.

110. Prevelige P and King J. (1993) "Assembly of Bacteriophage P22: A Model for ds-DNA Virus Assembly." In "Progress in Medical Virology, Vol. 40" (ed. J.L. Melnick) Karger, Basel, pp. 206-221.

111. Gordon C and King J. (1993) Temperature Sensitive Mutations in the P22 Coat Protein Which Interfere with Polypeptide Chain Folding. J. Biol. Chem., 268, 9358-9368.

112. King J. (1993) "The Unfolding Puzzle of Protein Folding." Technology Review, 96: 4, pp. 54-61.

113. Prasad BV, Prevelige PE, Marietta E, Chen RO, Thomas D, King J and Chiu W. (1993) Three-Dimensional Transformation of Capsids Associated with Genome Packaging in a Bacterial Virus. J. Mol. Biol., 231, 65-74.

114. Galisteo ML and King J. (1993) Conformational Transformations in the Protein Lattice of Phage P22 Procapsids. Biophysical Journal, 65, 227-235.

115. Teschke C and King J. (1993) Folding of the Phage P22 Coat Protein in vitro. Biochemistry, 32, 10839-10847.

116. Mitraki A, Danner M, King J and Seckler R. (1993) Temperature-sensitive Mutations and Second-site Suppressor Substitutions Affect Folding of the P22 Tailspike Protein in Vitro. J. Biol. Chem, 268, 20071-20075.

117. Teschke CM, King J and Prevelige PE Jr. (1993) Inhibition of capsid assembly by 1,1'-bi(4-anilino)naphthalene-5,5'-disulfonic acid. Biochemistry, 32, 10658-10665.

118. King, J., Teschke, C.M., Haase-Pettingell, C. and Mitraki, A. (1993) "Protein misfolding and inclusion body formation in prokaryotes." In: Research Opportunities in Biomolecular Engineering: The Interface Between chemical Engineering and Biology. Proceedings of the National Institute of General Medical Sciences. ( G. Georgiou and I. Glowinski, eds.), Washington, D.C., pp.25-32.

119. Gordon C and King J. (1994) Genetic properties of temperature sensitive folding mutants of the coat protein of phage P22. GENETICS, 136, 427-438.

120. Prevelige PE Jr, King J and Silva JL. (1994) Pressure denaturation of the bacteriophage P22 coat protain and its entropic stabilization in icosahedral shells. Biophys J., 66(5), 1631-1641.

121. Berger B, Shor PW, Tucker-Kellogg L and King J. (1994) A Local Rule Based Theory of Virus Shell Assembly. Proceedings of the National Academy of Sciences, 91, 7732-7736.

122. Friguet B, Djavadi-Ohaniance L, King J and Goldberg M. (1994) In Vitro and ribosome bound folding intermediates of P22 tailspike protein detected with monoclonal antibodies. J. Biol. Chem., 269, 15945-15949.

123. Sather S and King J. (1994) Intracellular Trapping of a Cytoplasmic folding Intermediate of the Phage P22 Tailspike Using Iodoacetamide. J. Biol. Chem., 269, 25268-25276.

124. Gordon C, Sather S, Casjens S and King J. (1994) Selective In Vivo Rescue by GroEL/ES of Thermolabile Folding Intermediates of Phage P22 Structural Proteins. J. Biol. Chem., 269, 27941-27951.

125. Greene B and King J. (1994) Binding of Scaffolding Subunits Within the P22 Procapsid Lattice.Virology, 205, 188-197.

126. Chen C-C, King J and Wang D. (1995) A Molecular Thermodynamic Model for Helix-Helix Docking and Protein Aggregation. AIChE Journal, 41, 1015-1024.

127. Teschke CM and King J. (1995) In Vitro folding of Phage P22 Coat Protein with Amino Acid Substitutions that Confer In Vivo Tempertature-Sensitivity. Biochemistry, 34, 6815-6826.

128. Speed MA, Wang DIC and King J. (1995) Multimeric Intermediates in the Pathway to the Aggregated Inclusion Body State for P22 Tailspike Polypeptide Chains. Protein Science, 4, 900-908.

129. Galisteo ML, Gordon CL and King J. (1995) Stability of Wild-Type and Temperature-Sensitive Protein Subunits of the Phage P22 Capsid. J. Biol. Chem., 270, 16595-16601.

130. King J, Haase-Pettingell C, Robinson A, Speed MA and Mitraki, A. (1996) Thermolabile Folding Intermediates: Inclusion Body Precursors and Chaperonin Substrates. FASEB Journal, 10, 57-66.

131. King J. (1996) Unexpected Pathways to protein stabilization. Nature Biotechnology, 14, 436.

132. Thuman-Commike P, Greene B, Jakana J, Prasad BVV, King J, Prevelige PE, Chiu W. (1996) Three-dimensional Structure of Scaffolding-containing Phage P22 Procapsids by Electron Cryo-microscopy. J. Mol. Biol., 260, 85-98.

133. Speed M, Wang D and King J. (1996) Specific aggregation of partially folded polypeptide chains: The molecular basis of inclusion body composition. Nature Biotechnology, 14, 1283-1287.

134. Greene B and King J. (1996) Scaffolding mutants identifying domains required for P22 procapsid assembly and maturation. Virology, 225, 82-96.

135. Speed M, Morshead T, Wang, DI and King J. (1997) Conformation of P22 tailspike folding and aggregation intermediates probed by monoclonal antibodies. Protein Science, 6, 99-108.

136. Haase-Pettingell C and King J. (1997) Prevalence of Temperature Sensitive folding Mutations in the parallel Beta Coil Domain of the Phage P22 Tailspike Endorhamnosidase. J. Mol. Biol., 267, 88-102.

137. King J and Chiu W. (1997) "The Procapsid to Capsid Transition in Double-stranded DNA Bacteriophages." In "Structural Biology of Viruses" (W. Chiu, R.M. Burnett and R. Garcea, eds.) Oxford University Press, pp. 288-311.

138. Speed M, King J and Wang DIC. (1997) Polymerization Mechanism of Polypeptide Chain Aggregation. Biotechnology and Bioengineering, 54, 333-343.

139. King J. (1997) "Refolding with a piece of the ring." Nature Biotechnology, 15, 7-8.

140. King J. (1997) "The Biotechnology Revolution: Self-replicating Factories and the Ownership of Life Forms." In "Cutting Edge: Technology, Information Capitalism and Social Revolution" (J. Davis, T. Hirschl and M. Stack, eds.) Verso Press, pp 145-156.

141. Robinson AS and King J. (1997) Disulfide-bonded intermediate on the folding and assembly pathway of a non-disulphide bonded protein. Nature Structural Biol., 4, 450-455.

142. Fan ZH, Jensen PK, King J and Lee CS. (1997) Monitoring the refolding pathway for a large multimeric protein using capillary zone electrophoresis. J. Chromatography, 769, 315-323.

143. Betts S, Haase-Pettingell C and King J. (1997) Mutational effects on inclusion body formation. In Protein Misassembly (ed. R. Wetzel), Volume 50 of "Advances in Protein Chemistry," Academic Press, pp 243-264.

144. Thuman-Commike, P.A., Greene, B., Malinski, J., King, J. and Chiu, W. (1998) Role of the Scaffolding Protein in P22 Procapsid Size Determination Suggested by T=4 and T=7 Procapsid Structures. Biophysical J., 74, 559-568.

145. Jensen, P.K., King, J. and Lee, C.S. (1998) Investigating temperature effects on refolding and aggregation of a large multimeric protein using capillary zone electrophoresis. Analytical Chemistry, 70, 730-736.

146. Liu CL, Kamei DT, King J, Wang DI and Blankschtein D. (1998) Separation of proteins and viruses using two-phase aqueous micellar systems. J. Chromatogr. B, 711, Nos. 1+2, pp. 127-138.

147. Betts, S. and King, J. (1998) Cold rescue of the thermolabile tailspike intermediate at the junction between producitve folding and off-pathway aggregation. Protein Sci., 7, 1516-1523.

148. Konz JO, King J and Cooney CL. (1998) Effects of oxygen on recombinant protein expression. Biotech. Progress, 14(3), 393-409.

149. King, J. (1998) public resources, not corporate property. The Environmental Forum, 14, 40-41.

150. Greene B and King J. (1999) In vitro unfolding/refolding of wild type phage P22 scaffolding protein reveals capsid binding domain." J. Biol. Chem., 274, 16135-16140.

151. Greene B and King J. (1999) Folding and stability of mutant scaffolding proteins defective in phage capsid assembly. J. Biol.Chem., 274, 16141-16146.

152. Istrail S, Schwartz R and King J. (1999) Lattice simulations of aggregation funnels for protein folding. J. of Computational Biology, 6, 143-162.

153. Thuman-Commike, P.A., Tsuruta, H., Greene, B., Prevelige, P.E., King, J. and Chiu, W. (1999) Solution X-ray scattering based estimation of electron cryomicroscopy imaging parameters for reconstruction of virus particles. Biophysical J., 76, 2249-2261.

154. King J and Stabinsky D. (1999) Biotechnology under globalisation: the corporate expropriation of plant, animal and microbial species. Race & Class, 40, 73-89.

155. King J and Stabinsky D. (1999) Patents on cells, genes, and organisms undermine the exchange of scientific ideas. The Chronicle of Higher Ed., Opinion & Arts, Feb. 5, 1999, pp. B6-B8.

156. Betts S and King J. (1999) There's a right way and a wrong way: in vivo and in vitro folding, misfolding and subunit assembly of the P22 tailspike. Structure, 7, R131-R139.

157. King J and Betts S. (1999) A green light for protein folding. Nature Biotech., 17, 637-638.

158. King, J. (1999) the scientific endeavor is based on vigilance, not trust. Science & Eng. Ethics, 5, 215-217.

159. Betts, S., Speed, M. and King, J. (1999) "Detection of early aggregation intermediates by native gel electrophoresis and native western blotting." In, Amyloid, Prions, and Other Protein Aggregates (ed. R. Wetzel), Vol. 309 of "Methods in Enzymology," Academic Press, pp. 333-350.

160. Ting C, Rocap G, King J and Chisholm SW. (1999) "Characterization of phycoerythrin genes in the chlorophyll a2/b2-containing prokaryote, Prochlorococcus sp. MIT9303." In: Photosynthesis: Mechanisms and Effects (G. Garab, ed.) Vol. I, Kluwer Academic Publishers, The Netherlands, pp. 225-228.

161. Pande A, Pande J, Aserie N, Lomakin A, Ogun O, King J, Lubsen N, Walton D and Benedek G. (2000) Molecular basis of a progresssive juvenile-onset hereditary cataract. PNAS, 97, 1993-1998.

162. Zhang Z, Greene B, Thuman-Commike PA, Jakana J, Prevelige PE, King J and Chiu W.(2000) Visualization of the maturation transition in bacteriophage P22 electron cryomicroscopy. J. Mol. Biol., 297, 615-626.

163. Raso SW and King J. (2000) "Protein folding and human disease." In, Protein Folding: Frontiers in Molecular Biology, 2nd Edition (ed. R. Pain), Oxford University Press, pp406-428.

164. Berger B, King J, Schwartz RS and Shor PW. (2000) Local Rule Mechanism for Selecting Icosahedral Shell Geometry. Discrete Applied Mathematics, 105, 55-69.

165. King J. (2000) "Environmental pollution and the emergence of new diseases." In, Environmental Evolution, 2nd Edition (ed. L. Margulis, C. Matthews & A. Haselton), MIT Press, pp 249-262.

166. Kreisberg JF, Betts SD and King J. (2000) β-helix core packing within the triple-stranded oligomerizatin domain of the P22 tailspike. Protein Science, 9, 2338-2343.

167. Haase-Pettingell C, Betts S, Raso SW, Stuart L, Robinson A and King J. (2001) Role for cysteine residues in the in vivo folding and assembly of the phage P22 tailspike. Protein Science, 10, 397-410.

168. Raso SW, Clark PL, Haase-Pettingell C, King J and Thomas GJ, Jr. (2001) Distinct cysteine sulfhydryl environments detected by analysis of Raman S-H markers of Cys —› Ser mutant proteins. J. Mol. Biol., 307, 899-911.

169. Schwartz, R., Istrail, S. And King, J. (2001) Frequencies of amino acid strings in globular protien sequences indicate suppression of blocks of consecutive hydrophobic residues. Protein Science, 10, 1023-1031.

170. Schwartz, R., Ting, C. and King, J. (2001) Whole proteome pI values correlate with subcellular localizations of proteins for organisms within the three domains of life. Genome Research, 11, 703-709.

171. Pande. A., Pande, J., Asherie, N., Lomakin, A., Ogun, O., King, J., and Benedek, G.B. (2001) Crystal cataracts: Human genetic cataract caused by protein crystallization. PNAS,98, 6116-6120.

172. Bradley, P., Cowen, L.J., Menke, M., King, J. and Berger, B. (2001) "Predicting the Beta-Helix Fold from Protein Sequence Data." In Proceedings of the Fifth Annual International Conference on Computational Molecular Biology, ACM Press, New York, pp. 59-67.

173. Clark, P.L. and King, J. (2001) A Newly Synthesized, Ribosome-Bound Polypeptide Chain adopts Conformations Dissimilar from Early In Vitro Refolding Intermediates. J. Biol.Chem., 276, 25411-25420.

174. Ting, C.S., Rocap, G., King, J. and Chisholm, S.W. (2001) Phycobiliprotein genes of the marine photosynthetic prokaryote Prochlorococcus: Evidence for rapid evolution of genetic heterogeneity. Microbiology, 147, 3171-3182 .

175. Bradley, P., Cowen, L., Menke, M., King, J. and Berger, B. (2001) BetaWrap: Successful prediction of parallel ß-helices from primary sequence reveals an association with many microbial pathogens. PNAS, 98, 14819-14824.

176. Asherie N, Pande J, Pande A, Zarutskie JA, Lomakin J, Lomakin A, Ogun O, Stern LJ, King J, Benedek GB. (2001) Enhanced Crystallization of the Cys18 to Ser Mutant of Bovine gammaB Crystallin. J. Mol.Biol., 314, 663-669.

177. Ting, C., Rocap, G., King, J. and Chisholm, S.W. (2002) Cyanobacterial photosynthesis in the oceans: the origins and significance of divergent light-harvesting strategies. Trends in Microbiology, 10, 134-142.

178. Kreisberg JF, Betts SD, Haase-Pettingell C. and King J. (2002) The interdigitated beta-helix domain of the P22 tailspike protein acts as a molecular clamp in trimer stabilization. Protein Science, 11, 820-830 .

179. Benton CB, Clark PL and King J. (2002) Characterization of the protrimer intermediate in the folding pathway of the interdigitated ß-helix tailspike protein. Biochemistry, 41:5093-5103.

180. Kamei D, Liu C, Haase-Pettingell C, King J, Wang DIC and Blankschtein D. (2002) Understanding viral partitioning in two-phase aqueous nonionic micellar systems: 1. Role of attractive interactions between viruses and micelles. Biotech & Bioeng, 78, 190-202.

181. Kamei D, King J, Wang DI and Blankschtein D. (2002) Understanding viral partitioning in two-phase aqueous nonionic micellar systems: 2.Effect of entrained micelle-poor domains. Biotech & Bioeng, 78, 203-216.

182. Cowen L, Bradley P, Menke M, King J and Berger B. (2002) Predicting the Beta-helix fold from protein sequence data. J. Comp. Biol., 9, 261-276.

183. King J, Haase-Pettingell C & Gossard D. (2002) Protein Folding and Misfolding. American Scientist, 90, 445-453.

184. Kamei D, King J, Wang DIC & Blankschtein D. (2002) Separating lysozyme from bacteriophage P22 in two-phase aqueous micellar systems. Biotech & Bioeng, 80, 233-236.

185. Griffiths SW, King J & Cooney CL. (2002) The reactivity and oxidation pathway of Cysteine 232 in Recombinant human α1-Antitrypsin. J. Biol. Chem., 277, 25486-25492.

186. Kosinski-Collins M & King J. (2003) In vitro unfolding and refolding of human gamma-D crystallin, a protein involved in cataract formation. Protein Science, 12, 480-490.

187. Weigele PR, Scanlon E and King J. (2003) Homo-trimeric, β-stranded viral adhesins and tail proteins. J. Bacteriology, 185, 4022-4030.

188. Menke M, Scanlon E, King J, Berger B and Cowen L. (2004) Wrap and Pack: A New Paradigm for Beta Structural Motif Recognition with Application to Recognizing Beta Trefoils. In Proceedings of the 8th Annual International Conference on Research in Computational Molecular Biology RECOMB, (P.E.Bourne and D. Gusfield, eds.). ACM Press, New York, pp. 298-307.

189. Kosinski-Collins M, Flaugh S & King J. (2004) Probing folding and fluorescence quenching in Human γD crystallin Greek key domains using Triple Tryptophan mutant proteins. Protein Science, 13, 2223-2235.

190. Pope W, Haase-Pettingell C & King J. (2004) Protein folding failure sets the high-temperature limit on the growth of phage P22 in Salmonella enterica serovar Typhimurium. Applied & Environmental Microbiology, 70(8), 4840-4847.

191. Betts S, Haase-Pettingell C, Cook K and King J. (2004) Buried hydrophobic side chains essential for the folding of the parallel β-helix domains of the P22 tailspike. Protein Science, 13, 2291-2303.

192. Flaugh SL, Kosinski-Collins MS and King J. (2005) Contributions of hydrophobic domain interface interactions to the folding and stability of human γD-crystallin. Protein Science, 14, 569-581.

193. Jain M, Evans MS, King J and Clark PL. (2005) Monoclonal antibody epitope mapping describes tailspike β-helix folding and aggregation intermediates. J.Biol.Chem., 280, 23032-23040.

194. Gossard DC and King J. (2005) Lattice transformations and subunit conformational changes in phage capsid maturation. J. of Theoretical Med., 6, 99-105.

195. Flaugh SL, Kosinski-Collins MS and King J. (2005) Interdomain side-chain interactions in human γD crystallin influencing folding and stability. Protein Science, 14, 2030-2043.

196. Menke M, Scanlon E, King J, Berger B and Cowen L. (2005) Wrap and Pack: A New Paradigm for Beta Structural Motif Recognition with Application to Recognizing Beta Trefoils. J.Computational Biol., 12: 777-795.

197. Raso SW, Abel J, Barnes JM, Maloney KM, Pipes G, Treuheit MJ, King J and Brems DN. (2005) Aggregation of graulocyte-colony stimulating factor in vitro involves a conformationally altered monomeric state. Protein Science, 14, 2246-2257.

198. Weigele P, Haase-Pettingell C, Campbell PG, Gossard DC and King J. (2005) Stalled folding mutants in the triple β-helix domain of the phage P22 tailspike adhesin. J.Mol.Biol., 354, 1103-1117.

199. Jiang W, Chang J, Jakana J, Weigele P, King J and Chiu W. (2006) Structure of Epsilon 15 bacteriophage reveals genome organization and DNA packaging/injection apparatus. Nature, 439, 612-616.

200. Schwartz R & King J. (2006) Frequencies of hydrophobic and hydrophilic runs and alternations in proteins of known structure. Protein Science, 15, 102-112.

201. Simkovsky R and King J. (2006) An elongated spine of buried core residues necessary for in vivo folding of the parallel β-helix of P22 tailspike adhesin. PNAS, 103, 3575-3580.

202. Chang J, Weigele P, King J, Chiu W and Jiang W. (2006) Cry-EM symmetric reconstruction of bacteriophage P22 reveals organization of its DNA packaging and infecting machinery. Structure, 14, 1073-1082.

203<. Chen J, Flaugh SL, Callis PR and King J. (2006) Mechanism of the highly efficient quenching of tryptophan fluorescence in human γ-D-crystallin. Biochemistry, 45, 11552-11563.

204. Flaugh SL, Mills IA and King J. (2006) Glutamine deamidation destabilizes human γD-crystallin and lowers the kinetic barrier to unfolding. J.Biol.Chem., 281, 30782-30793.

205. McDonnell AV, Menke M, Palmer N, King J, Cowen L and Berger B. (2006) Fold recognition and accurate sequence-structure alignment of sequences directing β-sheet proteins. Proteins, 63, 976-985.

206. Pope WH, Weigele PR, Chang J, Pedulla ML, Ford ME, Houtz JM, Jiang W, Chiu W, Hatfull GF, Hendrix RW and King JA. (2007), Genome sequence, structural proteins, and capsid organization of the cyanophage Syn5: a "horned" bacteriophage of marine Synechococcus. J. Mol. Biol., 368, 966-981.

207. Weigele PR, Pope WH, Pedulla ML, Houtz JM, Smith AL, King J, Hatfull GF, Lawrence JG and Hendrix RW. (2006) Genomic and structural analysis of Syn9, a cyanophage infecting marine prochlorococcus and synechococcus. Environmental Microbiology, 9, 1675-1695.

208. Papanikolopoulou K, Mills IA, Flaugh SL, Wang Y, Gross AAR, Kirschner DA, Decatur SM and King JA. (2007) Formation of Amyloid Fibrils In Vitro by Human γD-crystallin and its Isolated Domains. Molecular Vision, 14, 81-89.

209. Mills IA, Flaugh SL, Kosinski-Collins MS and King J. (2007) Folding and stability of the isolated greek key domains of the long-lived human lens proteins, γD-crystallin and γS-crystallin. Protein Science, 16, 2427-44.

210. King J. (2007) The High Stakes in Science Education: Risking the Roots of American Productivity. Education Week, 26, pgs. 34, 44.

211. Jiang W, Baker ML, Jakana J, Weigele PR, King J and Chiu W. (2008) Backbone structure of the infectious ε15 virus capsid revealed by electron cryomicroscopy. Nature, 451, 1130-1135.

212. Wang H, Duennwald ML, Roberts BE, Rozeboom LM, Zhang YL, Steele AD, Krishnan R, Su LJ, Griffin D, Mukhopadhyay S, Hennessy EJ, Weigele P, Blanchard BJ, King J, Deniz AA, Buchwald SL, Ingram VM, Lindquist SM and Shorter, J. (2008) Direct and selective elimination of specific prions and amyloids by 4,5-deanilinophthalimide and analogs. PNAS, 105, 7159-7164.

213. King J and Decatur S. (2008) Commentary: An Education on Higher Education for the Next President. Chronicle of Higher Education, 55/3, pg. A38. (Sept. 12, 2008)

214. Chen J, Toptygin D, Brand L and King J. (2008) Mechanism of the efficient tryptophan fluorescence quenching in human γD-crystallin studied by time-resolved fluorescence. Biochemistry, 47, 10705-10721.

215. Jung J, Byeon I-JL, Wang Y, King J and Gronenborn AM. (2009) The structure of the cataract-causing P23T mutant of Human γD-Crystallin exhibits local distinctive conformational and dynamic changes. Biochemistry, 48, 2597-2609.

216. Chen J, Callis PR and King J. (2009) Mechanism of the very efficient quenching of tryptophan fluorescence in human γD- and γS-crystallins; the γ-crystallin fold may have evolved to protect tryptophan residues from ultraviolet photodamage. Biochemistry, 48, 3708-3716.

217. Xu J, Chen J, Toptygin D, Tcherkasskaya O, Callis P, King J, Brand L, Knutson J. (2009) Femtosecond Fluorescence Spectra of Tryptophan in Human γ-Crystallin Mutants: Site-Dependent Ultrafast Quenching. J.Am.Chem.Soc., 131(46), 16751-16757.

218. Moreau K and King J, (2009) Hydrophobic Core Mutations Associated with Cataract Development in Mice Destabilize Human γD-Crystallin. J.Biol.Chem, 284, 33285-33295.

219. Das P, King JA and Zhou R. (2010) β-strand interactions at the domain interface critical for the stability of human lens γD-crystallin. Protein Science, 19(1), 131-140.

220. Wang Y and King J. (2010) Cataract as a protein aggregation disease. In, Protein Misfolding Diseases: Current and Emerging Principles and Therapies (Marina Ramirez-Alvarado, Jeffrey W. Kelly, and Christopher M. Dobson, eds.) John Wiley and Sons, Hoboken, NJ, pp 487-515.

221. Wang Y, Petty SA, Trojanowski A, Knee KM, Goulet D, Mukerji I and King JA. (2010) Formation of amyloid fibrils in vitro from partially unfolded intermediates of Human γC-Crystallin. IOVS, 51, 672-678.

222. Acosta-Sampson L and King J. (2010) Partially folded aggregation intermediates of human γD, γC, and γS-Crystallin are recognized and bound by human αβ-Crystallin chaperone. J.Mol.Bio, 401, 134-152.

223. Murata K, Liu X, Danev R, Jakana J, Schmid MF, King J, Nagayama K, and Chiu W. (2010) Zernike phase contrast cryo-electron microscopy and tomography for structure determination at nanometer and subnanometer resolutions. Structure, 18(8), 903-12.

224. Chang JT, Schmid MF, Haase-Pettingell C, Weigele PR, King JA and Chiu W. (2010) Visualizing the structural changes of bacteriophage Epsilon15 and its Salmonella host during infection. J.Mol.Biol, 402, 731-740.

225. Dudek EJ, Lampi KJ, Lampi JA, Shang F, King J, Wang Y, and Taylor A. (2010) Ubiquitin proteasome pathway-mediated degradation of proteins: effects due to site-specific substrate deamidation. IOVS, 51, 4164-4173.

226. Pereira JH, Ralston CY, Douglas NR, Meyer D, Knee KM, Goulet DR, King JA, Frydman J and Adams PD. (2010) Crystal structures of a group II chaperonin reveal the open and closed states associated with the protein folding cycle. J. Biol. Chem., 285(36), 27958-27966.

227. Knee KM, Goulet DR, Zhang J, Chen B, Chiu W and King JA. (2011) The Group II chaperonin Mm-Cpn binds and refolds human γD Crystallin. Protein Science, 20, 30-41.

228. Raytcheva DA, Haase-Pettingell C, Piret JM and King J. (2011) Intracellular assembly of Cyanophage Syn5 proceeds through a scaffold-containing procapsid. J. Virology, 85, 2406-2415.

229. Chen D-H, Baker ML, Hryc CF. DiMaio F, Jakana J, Wu W, Dougherty M, Haase-Pettingell C, Schmid MF, Jiang W, Baker D, King JA and Chiu W. (2011) Structural basis for scaffolding-mediated assembly and maturation of a dsDNA virus. PNAS, 108, 1355-1360.

230. Kong F and King J. Contributions of aromatic pairs to the folding and stability of long-lived human γD-crystallin. (2011) Protein Science, 20, 513-528.

231. Goulet DR, Knee KM and King JA. (2011) Inhibition of unfolding and aggregation of lens protein human γD-crystallin by sodium citrate. Exp. Eye Res., 93(4): 371-381.

232. Das P, King JA and Zhou R. (2011) Aggregation of γ-Crystallin associated with human cataracts via domain swapping at the C-terminus β-strands. PNAS, 108, 10514-10519.

233. Pereira JH, Ralston CY, Douglas NR, Kumar R, Lopez T, McAndrew RP, Knee KM, King JA, Frydman J and Adams PD. (2012) Mechanism of nucleotide sensing in group II Chaperonins. EMBO J., 31, 731-740.

234. Moreau KL and King JA. (2012) Protein misfolding and aggregation in cataract disease and prospects for prevention. Trends in Mol. Med., 18(5), 273-282. Epub 2012 Apr 19.

235. Moreau KL and King JA. (2012) Cataract-causing defect of a mutant γ-Crystallin proceeds through an aggregation pathway which bypasses recognition by γ-Crystallin chaperone. PLOS One, 17(5), e37256. Epub 2012 May 24.

236. Carvalho CM, Kropinski AM, Lingohr EJ, Santos SB, King J and Azeredo J. (2012) The genome and proteome of a Campylobacter coli bacteriophage vB_CcoM-IBB_35 reveal unusual features. Virology J., 9: 35.

237. Takata T, Haase-Pettingell C and King J. (2012) The C-terminal cysteine annulus participates in auto-chaperone function for Salmonella phage P22 tailspike folding and assembly. Bacteriophage, 2(1), 36-49.

238. Knee K, Sergeeva OA and King J. (2013) Human TRiC complex purified from HeLa cells contains all eight CCT subunits and is active in vitro. Cell Stress and Chaperones, 18(2), 137-144. Aug 13, 2012 Epub ahead of print, DOI: 10.1007/s12192-012-0357-z.

239. Sergeeva OA, Chen B, Haase-Pettingell C, Ludtke SJ, Chiu W and King JA. (2013) Human CCT4 and CCT5 chaperonin subunits expressed in E. coli form biologically active homo-oligomers. J.Biol.Chem., 288, 17734-17744.

240. Xia Z, Yang Z, Huynh T, King JA and Zhou R. (2013) UV-radiation Induced Disruption of Dry-Cavities in Human γD-crystallin Results in Decreased Stability and Faster Unfolding. Nature Scientific Reports, 3, article 1560. doi:10.1038/srep01560

241. Zhu B, Tabor S, Raytcheva DA, Hernandez A, King JA and Richardson CC. (2013) The RNA polymerase of marine cyanophage Syn5. J.Biol.Chem., 288, 3545-3552. Doi:10.1074/jbc.M112.442350

242. Schafheimer N and King J (2013) Tryptophan Cluster Protects Human γD-Crystallin from Ultraviolet Radiation-Induced Photo-Aggregation In Vitro. Photochem Photobiol. 2013 May 20. [Epub ahead of print] doi: 10.1111/php.12096.

243. Baker ML, Hryc CF, Zhang Q, Wu W, Jakana J, Haase-Pettingell C, Afonine PV, Adams PD, King JA, Jiang W, Chiu W. (2013) Validated near-atomic resolution structure of bacteriophage epsilon15 derived from cryo-EM and modeling. PNAS, 110(30), 12301-12306.

244. Dai W, Fu C, Raytcheva D, Flanagan J, Khant HA, Liu X, Rochat RH, Haase-Pettingell C, Piret J,  Ludtke SJ, Nagayama K, Schmid MF, King JA and Chiu W. (2013) Visualizing Virus Assembly Intermediates Inside Marine Cyanobacteria. Nature, 502, 707-710.

245. Yang Z, Xia Z, Huynh T, King JA and Zhou R. (2013) Dissecting the contributions of b-hairpin tyrosine pairs to the folding and stability of long-lived human γD-crystallins. Nanoscale, doi:10.1039/c3nr03782g. (Royal Society of Chemistry)

246. Raytcheva DA, Haase-Pettingell C, Piret J, King JA. (2014) " target="_blank">Two Novel Proteins of Cyanophage Syn5 Compose Its Unusual Horn Structure. J Virol., 88, 2047-2055. [2013 Dec 4. Epub ahead of print]

247. Schafheimer N, Wang Z, Schey K and King J. (2014) " target="_blank">Tryosine/Cysteine cluster sensitizing human γD-Crystallin to ultraviolet radiation-induced photo-aggregation in vitro. Biochemistry, 53(6), 979-990.

248. Sergeeva OA, Yang J, King JA, and Knee KM. (2014) Group II archaeal chaperonin recognition of partially folded human γD crystallin mutants. Protein Sci March 10 doi: 10.1002/pro.2452. [Epub ahead of print]

249. Serebryany E, and King JA (2014) The βγ-crystallins: Native state stability and pathways to aggregation. Prog Biophys and Mol Biol ("Crystallins of the Eye"), accepted.

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