Linked Life Data

8643385

Source:http://linkedlifedata.com/resource/pubmed/id/8643385

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
33
pubmed:dateCreated
1996-7-17
pubmed:abstractText
We want to understand how environmental factors influence zymogen activation of the "cloaked' active site of the 'Ribosome Inactivating Protein' (RIP) from corn kernels. In this study, we focus on how likely chemical effectors in the immediate environment of the 'lid' conspire to unleash the active site upon encountering target membranes of invading pests. Octanol-H2O partitioning free energies of peptides which (i) straddle the proteolysis site, and (ii) form the 'side' and 'bottom' of the proposed 'lid' were found to only slightly favor H2O, suggesting that the peptide is poised to detach from the less polar surface surrounding the RIP active site. Circular dichroism results obtained upon catalase/H2O2 oxidation of the 'lid' peptide suggest that the structure shifts from primarily alpha-helical to primarily beta-like. These results suggest that the active site is more easily 'uncloaked' as a result of the lowered solvent polarity conditions and higher oxidant concentrations in the presence of pest membranes encountered during crucial stages of seed germination.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0261-3166
pubmed:author
pubmed:issnType
Print
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
249-53
pubmed:dateRevised
2011-6-6
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Factors affecting activation of the 'cloaked' Zea maize ribosome inactivating protein (RIP) zymogen. 1. 'LID' peptide hydrophobicities and oxidative structural changes.
pubmed:affiliation
Department of Biochemistry, North Carolina State University, Raleigh 27695, USA.
pubmed:publicationType
Journal Article