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Kang, Sebyung
Protein Nanobio Lab
Research Interests
  • Protein engineering, Drug/diagnostics delivery nanoplatform, Protein-based vaccine delivery systems, Biosensor & imaging

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Domain study of bacteriophage P22 coat protein and characterization of the capsid lattice transformation by hydrogen/deuterium exchange

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dc.contributor.author Kang, Sebyung ko
dc.contributor.author Prevelige, PE ko
dc.date.available 2014-09-29T01:35:19Z -
dc.date.created 2014-09-23 ko
dc.date.issued 2005-04 ko
dc.identifier.citation JOURNAL OF MOLECULAR BIOLOGY, v.347, no.5, pp.935 - 948 ko
dc.identifier.issn 0022-2836 ko
dc.identifier.uri https://scholarworks.unist.ac.kr/handle/201301/6547 -
dc.description.abstract Viral capsids are dynamic structures which undergo a series of structural transformations to form infectious viruses. The dsDNA bacteriophage P22 is used as a model system to study the assembly and maturation of icosahedral dsDNA viruses. The P22 procapsid, which is the viral capsid precursor, is assembled from coat protein with the aid of scaffolding protein. Upon DNA packaging, the capsid lattice expands and becomes a stable virion. Limited proteolysis and biochemical experiments indicated that the coat protein consists of two domains connected by a flexible loop. To investigate the properties and roles of the sub-domains, we have cloned them and initiated structure and function studies. The N-terminal domain, which is made up of 190 amino acid residues, is largely unstructured in solution, while the C-terminal domain, which consists of 239 amino acid residues, forms a stable non-covalent dimer. The N-terminal domain adopts additional structure in the context of the C-terminal domain which might form a platform on which the N-terminal domain can fold. The local dynamics of the coat protein in both procapsids and mature capsids was monitored by hydrogen/deuterium exchange combined with mass spectrometry. The exchange rate for C-terminal domain peptides was similar in both forms. However, the N-terminal domain was more flexible in the empty procapsid shells than in the mature capsids. The flexibility of the N-terminal domain observed in the solution persisted into the procapsid form, but was lost upon maturation. The loop region connecting the two domains exchanged rapidly in the empty procapsid shells, but more slowly in the mature capsids. The global stabilization of the N-terminal domain and the flexibility encoded in the loop region may be a key component of the maturation process. ko
dc.description.statementofresponsibility close -
dc.language 영어 ko
dc.publisher ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD ko
dc.title Domain study of bacteriophage P22 coat protein and characterization of the capsid lattice transformation by hydrogen/deuterium exchange ko
dc.type ARTICLE ko
dc.identifier.scopusid 2-s2.0-15244356061 ko
dc.identifier.wosid 000228111800006 ko
dc.type.rims ART ko
dc.description.wostc 28 *
dc.description.scopustc 26 *
dc.date.tcdate 2015-05-06 *
dc.date.scptcdate 2014-09-23 *
dc.identifier.doi 10.1016/j.jmb.2005.02.021 ko
dc.identifier.url http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=15244356061 ko
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