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X-ray diffraction analysis of gene V protein encoded by filamentous bacteriophage Ff
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http://hdl.handle.net/2142/20593
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| Title: | X-ray diffraction analysis of gene V protein encoded by filamentous bacteriophage Ff |
| Author(s): | Zhang, Hong |
| Doctoral Committee Chair(s): | Wang, Andrew H.-J |
| Department / Program: | Biophysics and Computational Biology |
| Discipline: | Biophysics |
| Degree Granting Institution: | University of Illinois at Urbana-Champaign |
| Degree: | Ph.D. |
| Genre: | Dissertation |
| Subject(s): |
Chemistry, Biochemistry
Biophysics, General |
| 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. 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. |
| Issue Date: | 1994 |
| Type: | Text |
| Language: | English |
| URI: | http://hdl.handle.net/2142/20593 |
| Rights Information: | Copyright 1994 Zhang, Hong |
| Date Available in IDEALS: | 2011-05-07 |
| Identifier in Online Catalog: | AAI9512607 |
| OCLC Identifier: | (UMI)AAI9512607 |
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Graduate Theses and Dissertations at Illinois
Graduate Theses and Dissertations at Illinois -
Dissertations - Biophysics and Computational Biology
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