| pubmed-article:8388289 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8388289 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:8388289 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:8388289 | pubmed:dateCreated | 1993-6-24 | lld:pubmed |
| pubmed-article:8388289 | pubmed:abstractText | Charge substitutions generated by site-directed mutagenesis at the termini of adjacent anti-parallel alpha-helices in a four-helix bundle protein were used to determine a precise value for the contribution of indirect charge-charge interactions to overall protein stability, and to simulate the electrostatic effects of alpha-helix macrodipoles. Thermodynamic double mutant cycles were constructed to measure the interaction energy between such charges on adjacent anti-parallel helices in the four-helix bundle cytochrome b562 from Escherichia coli. Previously, theoretical calculations of helix macrodipole interactions using modeled four-helix bundle proteins have predicted values ranging over an order of magnitude from 0.2 to 2.5 kcal/mol. Our system represents the first experimental evidence for electrostatic interactions such as those between partial charges due to helix macrodipole charges. At the positions mutated, we have measured a favorable interaction energy of 0.6 kcal/mol between opposite charges simulating an anti-parallel helix pair. Pairs of negative or positive charges simulating a parallel orientation of helices produce an unfavorable interaction of similar magnitude. The interaction energies show a strong dependence upon ionic strength, consistent with an electrostatic effect. Indirect electrostatic contacts do appear to confer a limited stabilization upon the association of anti-parallel packing of helices, favoring this orientation by as much as 1 kcal/mol at 20 mM K phosphate. | lld:pubmed |
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| pubmed-article:8388289 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8388289 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8388289 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:8388289 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8388289 | pubmed:month | May | lld:pubmed |
| pubmed-article:8388289 | pubmed:issn | 0961-8368 | lld:pubmed |
| pubmed-article:8388289 | pubmed:author | pubmed-author:SligarS GSG | lld:pubmed |
| pubmed-article:8388289 | pubmed:author | pubmed-author:RobinsonC RCR | lld:pubmed |
| pubmed-article:8388289 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8388289 | pubmed:volume | 2 | lld:pubmed |
| pubmed-article:8388289 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8388289 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8388289 | pubmed:pagination | 826-37 | lld:pubmed |
| pubmed-article:8388289 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:8388289 | pubmed:year | 1993 | lld:pubmed |
| pubmed-article:8388289 | pubmed:articleTitle | Electrostatic stabilization in four-helix bundle proteins. | lld:pubmed |
| pubmed-article:8388289 | pubmed:affiliation | Department of Biochemistry, University of Illinois, Urbana 61801. | lld:pubmed |
| pubmed-article:8388289 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8388289 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:8388289 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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