Linked Life Data

8267612

Source:http://linkedlifedata.com/resource/pubmed/id/8267612

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1994-1-25
pubmed:abstractText
The Fourier-transform infrared (FT-IR) spectra in trifluoroethanol (TFE) of phosphorylated peptides, NF-M17(Ser6P) and NF-M17(Ser11P) representing the C-terminal repeating domain of the midsized neurofilament protein subunit (NF-M) have been measured. In the absence of Ca2+ ions both phosphopeptides adopt predominantly aperiodic conformation with minor amounts of beta-turns, 3(10) helix or beta-pleated sheet. Addition of Ca(ClO4)2 results in opaque solutions, and in the case of the Ser6P peptide, precipitation. The infrared spectra of the supernatants reflect the presence of unordered and beta-sheet structure. The infrared spectrum of the solid Ca(2+)-complex of NF-M17 (Ser6P) in a KBr pellet shows amide component bands at 1654 (alpha-helix or loops) and 1626.5 cm-1 (beta-sheet). The high intensity of the beta-sheet component suggests extensive beta-aggregation. The data reported herein give an infrared spectroscopic support to our previous findings that upon Ca2+ binding, phosphorylated NF-M fragments undergo a marked conformational change which gives rise to partial beta-sheet formation and beta-aggregation. This observation may have relevance to the molecular events which lead to the accumulation of abnormal proteineous structures in Alzheimer's disease.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
197
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
755-62
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
FT-IR spectroscopy indicates that Ca(2+)-binding to phosphorylated C-terminal fragments of the midsized neurofilament protein subunit results in beta-sheet formation and beta-aggregation.
pubmed:affiliation
Central Research Institute of Chemistry, Budapest, Hungary.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't