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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
3
|
| pubmed:dateCreated |
1997-12-2
|
| pubmed:abstractText |
The aggregation and structural properties of the synthetic C-terminal half [Ala330, Ala350(270-373; 104-mer)] polypeptide from HIV-1 p24gag were studied. In concentrated solutions the synthetic polypeptide aggregated to tetramers which, upon dilution, gave a mixture of monomeric and dimeric and dimeric species. These results correlated well with the in vitro aggregation properties of recombinant p24. The tetrameric form of the synthetic polypeptide had a pI which differed by about four units from that of the mixture of monomeric and dimeric species. CD studies indicated that the latter contained, in aqueous solutions, a compact molecule lacking, however, a defined tertiary structure. Addition of MeOH to aqueous solutions of both tetramer and monomer/dimer mixture induced a more defined structure, which was assigned to that of an alpha + beta protein in agreement with secondary structure predictions. A model of the dimeric form of the 104-mer, which takes into account the results presented here and those from a study on the specificity of a set of anti-104-mer MoAbs, is presented. Finally, the results indicated that the structure of the 104-mer in its dimeric form is similar to that adopted by the same sequence when part of full-length p24.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:issn |
1075-2617
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
3
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
168-80
|
| pubmed:dateRevised |
2001-11-13
|
| pubmed:meshHeading |
pubmed-meshheading:9230482-Amino Acid Sequence,
pubmed-meshheading:9230482-Chromatography, Gel,
pubmed-meshheading:9230482-Chromatography, High Pressure Liquid,
pubmed-meshheading:9230482-Chromatography, Ion Exchange,
pubmed-meshheading:9230482-Circular Dichroism,
pubmed-meshheading:9230482-HIV Core Protein p24,
pubmed-meshheading:9230482-HIV-1,
pubmed-meshheading:9230482-Isoelectric Focusing,
pubmed-meshheading:9230482-Molecular Sequence Data,
pubmed-meshheading:9230482-Peptide Fragments,
pubmed-meshheading:9230482-Peptides,
pubmed-meshheading:9230482-Protein Conformation,
pubmed-meshheading:9230482-Protein Structure, Secondary,
pubmed-meshheading:9230482-Sequence Alignment
|
| pubmed:articleTitle |
The structural and aggregation properties of the synthetic C-terminal half (104-mer) polypeptide from HIV p24gag resemble those of full-length protein.
|
| pubmed:affiliation |
Italfarmaco Research Centre, Cinisello Balsamo, Milan, Italy.
|
| pubmed:publicationType |
Journal Article
|