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oai:www.ideals.illinois.edu:2142/20593 2023-07-10 col_2142_5131 col_2142_14828 com_2142_5130 com_2142_14827 com_2142_14793 com_2142_8903

Wang, Andrew H.J. Zhang, Hong 2011-05-07T12:43:42Z 2011-05-07T12:43:42Z 10000-01-01 1994 The gene V protein encoded by bacteriophage Ff is a single-stranded DNA binding protein and it plays an important role in the replication cycle of the phage. The crystal structure of the gene V protein was determined using multiwavelength anomalous diffraction on the selenomethionine-containing wild-type and isoleucine-47 $\to$ methionine mutant proteins with x-ray diffraction data phased to 2.5 A resolution. The structure of the wild-type protein was refined to an R factor of 19.1% using native data to 1.8 A resolution. The gene V protein monomer is largely composed of $\beta$-structures, including a distorted five stranded antiparallel $\beta$-barrel and two prominent extended $\beta$-hairpins. The two monomers are closely associated together to form a dimer. The DNA binding site of the protein was explored by the qualitative electrostatic potential calculations. The result from the preliminary x-ray diffraction analysis of co-crystals of gene V protein and oligonucleotides was also presented. The crystal structures of four mutant gene V proteins were solved and refined to $\sim$2 A resolutions. Three of these mutants were apolar substitutions in the hydrophobic core of the protein. One mutant, Arg 82 $\to$ Cys, is at the protein surface and is involved in breaking up of a surface salt bridge. The effects of these substitutions on the stability of the protein were discussed. Made available in DSpace on 2011-05-07T12:43:42Z (GMT). No. of bitstreams: 2 license.txt: 4922 bytes, checksum: 910b249b4beec47e7ab768910c8f966f (MD5) 9512607.pdf: 4471906 bytes, checksum: 2ebbbd30b5873b3cfe08a49b2bcaf99e (MD5) Previous issue date: 1994 Item marked as restricted to the 'UIUC Users [automated]' Group (id=2) by Howard Ding (hding2@illinois.edu) on 2011-05-07T14:44:56Z Item is restricted indefinitely. Restriction data tranferred 2014-07-01T11:19:50-05:00 Original Data Group with Access UIUC Users [automated] Release Date: none Reason: ETDs are only available to UIUC Users without author permission ETDs are only available to UIUC Users without author permission U of I Only AAI9512607 (UMI)AAI9512607 http://hdl.handle.net/2142/20593 eng Copyright 1994 Zhang, Hong Chemistry, Biochemistry Biophysics, General X-ray diffraction analysis of gene V protein encoded by filamentous bacteriophage Ff text Biophysics and Computational Biology Biophysics University of Illinois at Urbana-Champaign Dissertation Ph.D.