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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

Cited 28 times inthomson ciCited 26 times inthomson ci
Title
Domain study of bacteriophage P22 coat protein and characterization of the capsid lattice transformation by hydrogen/deuterium exchange
Author
Kang, SebyungPrevelige, PE
Issue Date
2005-04
Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
Citation
JOURNAL OF MOLECULAR BIOLOGY, v.347, no.5, pp.935 - 948
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.
URI
https://scholarworks.unist.ac.kr/handle/201301/6547
URL
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=15244356061
DOI
10.1016/j.jmb.2005.02.021
ISSN
0022-2836
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BIO_Journal Papers
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