| pubmed-article:1691014 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1691014 | lifeskim:mentions | umls-concept:C0002812 | lld:lifeskim |
| pubmed-article:1691014 | lifeskim:mentions | umls-concept:C0220781 | lld:lifeskim |
| pubmed-article:1691014 | lifeskim:mentions | umls-concept:C0872192 | lld:lifeskim |
| pubmed-article:1691014 | lifeskim:mentions | umls-concept:C2003941 | lld:lifeskim |
| pubmed-article:1691014 | lifeskim:mentions | umls-concept:C1521761 | lld:lifeskim |
| pubmed-article:1691014 | lifeskim:mentions | umls-concept:C1883254 | lld:lifeskim |
| pubmed-article:1691014 | lifeskim:mentions | umls-concept:C0005553 | lld:lifeskim |
| pubmed-article:1691014 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:1691014 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:1691014 | pubmed:dateCreated | 1990-5-17 | lld:pubmed |
| pubmed-article:1691014 | pubmed:abstractText | Model peptides with predetermined secondary, tertiary, and quaternary conformation have been successfully designed, synthesized, and characterized in an attempt to mimic the three-dimensional structure of an antigenic determinant. This work is a continuing effort to map the antigenic structure of the protein antigen lactate dehydrogenase C4 (LDH-C4) to develop a contraceptive vaccine. A putative topographic determinant with alpha alpha topology which associates into four-helix bundles was designed on the basis of the framework model of protein folding. An idealized amphiphilic 18-residue sequence (alpha 1) and a 40-residue alpha alpha fold (alpha 3) have been shown to form stable 4-helix structures in solution with a free energy of association on the order of -20.8 kcal/mol (tetramerization of alpha 1) and -7.8 kcal/mol (dimerization of alpha 3). Both alpha 1 and alpha 3 form stable monolayers at the air-water interface. The CD spectra of Langmuir-Blodgett monolayers are characteristically alpha-helical. Both CD and FTIR spectroscopic studies reval a high degree of secondary structure. The SAXS data strongly suggest that the helices are arranged in a four-helix bundle since the radius of gyration of 17.2 A and the vector distribution function are indicative of a prolate ellipsoid of axial dimensions and molecular weight appropriate for the four-helix bundle. The major contribution to the formation and stabilization of alpha 1 and alpha 3 is believed to be hydrophobic interaction between the amphiphilic alpha-helices. The displayed heptad repeat, helix dipole, ion pairs, and the loop sequence may have also contributed to the overall stability and antiparallel packing of the helices. A detailed structural analysis of a relevant topographic immunogenic determinant will elucidate the nature of antigen-antibody interactions as well as provide insight into protein folding intermediates. | lld:pubmed |
| pubmed-article:1691014 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1691014 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1691014 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1691014 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1691014 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1691014 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1691014 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1691014 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:1691014 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1691014 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1691014 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1691014 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:1691014 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:1691014 | pubmed:author | pubmed-author:GoldbergEE | lld:pubmed |
| pubmed-article:1691014 | pubmed:author | pubmed-author:TrewhellaJJ | lld:pubmed |
| pubmed-article:1691014 | pubmed:author | pubmed-author:KezdyF JFJ | lld:pubmed |
| pubmed-article:1691014 | pubmed:author | pubmed-author:KaumayaP TPT | lld:pubmed |
| pubmed-article:1691014 | pubmed:author | pubmed-author:BerndtK DKD | lld:pubmed |
| pubmed-article:1691014 | pubmed:author | pubmed-author:HeidornD BDB | lld:pubmed |
| pubmed-article:1691014 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1691014 | pubmed:day | 9 | lld:pubmed |
| pubmed-article:1691014 | pubmed:volume | 29 | lld:pubmed |
| pubmed-article:1691014 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1691014 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1691014 | pubmed:pagination | 13-23 | lld:pubmed |
| pubmed-article:1691014 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:1691014 | pubmed:meshHeading | pubmed-meshheading:1691014-... | lld:pubmed |
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| pubmed-article:1691014 | pubmed:meshHeading | pubmed-meshheading:1691014-... | lld:pubmed |
| pubmed-article:1691014 | pubmed:meshHeading | pubmed-meshheading:1691014-... | lld:pubmed |
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| pubmed-article:1691014 | pubmed:meshHeading | pubmed-meshheading:1691014-... | lld:pubmed |
| pubmed-article:1691014 | pubmed:year | 1990 | lld:pubmed |
| pubmed-article:1691014 | pubmed:articleTitle | Synthesis and biophysical characterization of engineered topographic immunogenic determinants with alpha alpha topology. | lld:pubmed |
| pubmed-article:1691014 | pubmed:affiliation | Department of Biochemistry and Molecular Biology and Cell Biology, Northwestern University, Evanston, Illinois 60208. | lld:pubmed |
| pubmed-article:1691014 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1691014 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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