| pubmed-article:1848998 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1848998 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:1848998 | lifeskim:mentions | umls-concept:C0220781 | lld:lifeskim |
| pubmed-article:1848998 | lifeskim:mentions | umls-concept:C1516692 | lld:lifeskim |
| pubmed-article:1848998 | lifeskim:mentions | umls-concept:C1883254 | lld:lifeskim |
| pubmed-article:1848998 | lifeskim:mentions | umls-concept:C0037812 | lld:lifeskim |
| pubmed-article:1848998 | lifeskim:mentions | umls-concept:C0596448 | lld:lifeskim |
| pubmed-article:1848998 | pubmed:issue | 13 | lld:pubmed |
| pubmed-article:1848998 | pubmed:dateCreated | 1991-5-3 | lld:pubmed |
| pubmed-article:1848998 | pubmed:abstractText | Receptor-adhesive modular proteins are nongenetic proteins designed to contain ligand, spacer, coil, and linker modules and to interact strongly with integrins or other types of cell-surface receptors. We have designed, chemically synthesized, and characterized a 39-residue peptide chain having a 6-residue ligand module (Gly-Arg-Gly-Asp-Ser-Pro-) for adherence to Arg-Gly-Asp-binding integrin receptors, a 3-residue spacer module (-Gly-Tyr-Gly-) for flexibility, and a 30-residue coil module [-(Arg-Ile-Glu-Ala-Ile-Glu-Ala) 4-Arg-Cys-NH2] containing four 7-residue repeats for dimerization. This chain was designed to form a 78-residue noncovalent dimer (P39) by folding the coils of two chains into an alpha-helical coiled coil through hydrophobic interaction of eight pairs of Ile residues. Air oxidation of P39 gave P78, a 78-residue covalent dimer having a disulfide bridge linking its C termini. Raman spectroscopy indicated that both synthetic proteins have high alpha-helical content. Ultraviolet circular dichroic spectroscopy indicated that both dimers contain stable alpha-helical coiled coils. Its C-terminal disulfide bridge renders P78 significantly more stable than P39 to thermal denaturation or denaturation by urea. The coiled coil of P39 was 30% unfolded near 55 degrees C and half-unfolded in 8 M urea, while that of P78 was 30% unfolded only near 85 degrees C. These studies have demonstrated the feasibility of using these ligand, spacer, and coil modules to construct the designed coiled-coil proteins P39 and P78, a stage in the nanometric engineering of receptor-adhesive modular proteins. | lld:pubmed |
| pubmed-article:1848998 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1848998 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1848998 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1848998 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1848998 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1848998 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:1848998 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1848998 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:1848998 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:1848998 | pubmed:author | pubmed-author:EricksonB WBW | lld:pubmed |
| pubmed-article:1848998 | pubmed:author | pubmed-author:WilliamsR WRW | lld:pubmed |
| pubmed-article:1848998 | pubmed:author | pubmed-author:EngelMM | lld:pubmed |
| pubmed-article:1848998 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1848998 | pubmed:day | 2 | lld:pubmed |
| pubmed-article:1848998 | pubmed:volume | 30 | lld:pubmed |
| pubmed-article:1848998 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1848998 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1848998 | pubmed:pagination | 3161-9 | lld:pubmed |
| pubmed-article:1848998 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:1848998 | pubmed:meshHeading | pubmed-meshheading:1848998-... | lld:pubmed |
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| pubmed-article:1848998 | pubmed:meshHeading | pubmed-meshheading:1848998-... | lld:pubmed |
| pubmed-article:1848998 | pubmed:year | 1991 | lld:pubmed |
| pubmed-article:1848998 | pubmed:articleTitle | Designed coiled-coil proteins: synthesis and spectroscopy of two 78-residue alpha-helical dimers. | lld:pubmed |
| pubmed-article:1848998 | pubmed:affiliation | Department of Chemistry, University of North Carolina, Chapel Hill 27599-3290. | lld:pubmed |
| pubmed-article:1848998 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1848998 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:1848998 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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