A study of the acid molten globule state of the histidine-containing proteins (HPr) from Escherichia coli and Bacillus subtilis /
anion and its electron distribution, iv) the environment of
| Main Author: | |
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| Format: | Thesis eBook |
| Language: | English |
| Published: |
[Place of publication not identified] :
[publisher not identified] ;
1997.
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| Subjects: | |
| Online Access: | Link to OAKTrust copy |
| Summary: | anion and its electron distribution, iv) the environment of at 25 'C by far-UV circular dichroism (CD) and fluorescence Bacillus subtilis and two mutants from the ecHPr protein, by which anions produce the IA state involves: i) charge concentrations of the transition indicate that the mechanism cosolvent (fluorescent probes). histidine-containing proteins (HPr) from Escherichia coli, indicated by the far-UV CD and intrinsic fluorescence K45E and F22W by Na2SO4 and NaCl indicate these proteins monitored at 25 'C by intrinsic fluorescence of the more effective than the chloride anion in producing the IA naphthylamine) binding. The ecHPr F22W mutant was further of ANS (1-anilino-8-naphthalene sulfonate) and NPN (N-phenyl- refold to a compact intermediate (IA) with characteristics of screening, ii) water structuring, iii) the ionic size of the state. However, the refolding is not a two-state process as the molten globule. The salt-induced refolding was monitored the protein surface, and v) other conditions such as, another The salt-induced transition of the low pH forms of the transition curves of ecHPr F22W. The midpoint salt tryptophan fluorophore. In all cases, the sulfate anion was |
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| Item Description: | "Major subject: Biochemistry". Vita. |
| Physical Description: | xiv, 82 leaves : illustrations ; 28 cm. Also available online. Issued also on microfiche from Lange Micrographics. |
| Bibliography: | Includes bibliographical references: pages 77-81. |