{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/20593"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/20593","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"X-ray diffraction analysis of gene V protein encoded by filamentous bacteriophage Ff","abstract":"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.","abstract_html":"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 <span class=\"etd-inline-math\">&beta;</span>-structures, including a distorted five stranded antiparallel <span class=\"etd-inline-math\">&beta;</span>-barrel and two prominent extended <span class=\"etd-inline-math\">&beta;</span>-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.","abstract_has_math":true,"creators":["Zhang, Hong"],"institution":"University of Illinois at Urbana-Champaign","degree_name":"Ph.D.","degree_level":"Dissertation","degree_discipline":"Biophysics","degree_department":null,"school":null,"contributors":["Wang, Andrew H.J."],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2011,"date_issued":"2011-05-07T12:43:42Z","date_published":"2011-05-07T12:43:42Z","updated_at":"2026-07-22T22:25:16Z","subjects":["Chemistry, Biochemistry","Biophysics, General"],"languages":["eng"],"rights":["Copyright 1994 Zhang, Hong"],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["AAI9512607","(UMI)AAI9512607"],"render_values":[{"text":"AAI9512607","href":null,"code":true},{"text":"(UMI)AAI9512607","href":null,"code":true}]}]},"links":{"outbound_url":"http://hdl.handle.net/2142/20593","outbound_label":"Handle","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Wang, Andrew H.J."]},{"key":"dc:creator","label":"Author","values":["Zhang, Hong"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2011-05-07T12:43:42Z","10000-01-01","1994"]},{"key":"dc:type","label":"Dc Type","values":["text"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Biophysics"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Dissertation"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Ph.D."]},{"key":"thesis:institution_name","label":"Thesis Institution Name","values":["University of Illinois at Urbana-Champaign"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["Chemistry, Biochemistry","Biophysics, General"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language","label":"Dc Language","values":["eng"]},{"key":"dc:rights","label":"Dc Rights","values":["Copyright 1994 Zhang, Hong"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["AAI9512607","(UMI)AAI9512607","http://hdl.handle.net/2142/20593"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["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"]},{"key":"dc:title","label":"Title","values":["X-ray diffraction analysis of gene V protein encoded by filamentous bacteriophage Ff"]}]}],"canonical_facts":{"dc:contributor":["Wang, Andrew H.J."],"dc:creator":["Zhang, Hong"],"dc:date":["2011-05-07T12:43:42Z","10000-01-01","1994"],"dc:description":["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"],"dc:identifier":["AAI9512607","(UMI)AAI9512607","http://hdl.handle.net/2142/20593"],"dc:language":["eng"],"dc:rights":["Copyright 1994 Zhang, Hong"],"dc:subject":["Chemistry, Biochemistry","Biophysics, General"],"dc:title":["X-ray diffraction analysis of gene V protein encoded by filamentous bacteriophage Ff"],"dc:type":["text"],"thesis:degree_discipline":["Biophysics"],"thesis:degree_level":["Dissertation"],"thesis:degree_name":["Ph.D."],"thesis:institution_name":["University of Illinois at Urbana-Champaign"]},"updated_at":"2026-07-22T22:25:16Z"}