Thermodynamic characterization of Escherichia coli Single Strand Binding protein, Single-Stranded polynucleotide interactions /
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| Other Authors: | , , , |
| Format: | Thesis Book |
| Language: | English |
| Published: |
1989.
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| Subjects: | |
| Online Access: | Link to OAKTrust copy |
| Abstract: | The E. coli Single Strand Binding (SSB) protein is vital in DNA replication, recombination and repair. The dependence of the intrinsic association equilibrium constant K (subscript obs), and the ("tetramer/octamer") cooperatively parameter, [symbol in PDF], on salt concentration with poly (A), poly (U), poly (dA) and poly (dT), as well as ion type, pH and temperature with poly(U) are determined by titrations which monitor the fluorescence quenching of the SSB protein upon complex formation. The cooperatively parameter has a value of [symbol in PDF]= 410 (plus or minus sign) 120, independent of salt concentration and type for poly (dA), poly(U) and poly(A) (25°C, pH 8.1). K (subscript obs) decreases steeply with increasing NaCl concentration for these polynucleotides. K (subscript obs) for the SSB-poly (dT) interaction is NaBr concentration dependent while a salt-independent [symbol in PDF]=130 (plus or minus sign)70 is obtained. The SSB protein shows a marked polynucleotide specificity. A dramatic effect of anion type is observed for the SSB protein-poly (U) interaction indicating net anion release from the complex. Results of anion competition experiments suggest a minimum of five independent and identical anion binding sites. The primary effect of pH, studied from 5.5 to 9.0, for the SSB tetramer-poly(U) interaction is on K(subscript obs) but [symbol in PDF] is pH dependent also.. |
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| Item Description: | Typescript (photocopy). Vita. "Major subject: Biochemistry." |
| Physical Description: | xv, 181 leaves : illustrations ; 29 cm |
| Bibliography: | Includes bibliographical references. |