Source:http://linkedlifedata.com/resource/pubmed/id/14982446
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
8
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| pubmed:dateCreated |
2004-2-25
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| pubmed:abstractText |
The application of Raman spectroscopy to characterize natively unfolded proteins has been underdeveloped, even though it has significant technical advantages. We propose that a simple three-component band fitting of the amide I region can assist in the conformational characterization of the ensemble of structures present in natively unfolded proteins. The Raman spectra of alpha-synuclein, a prototypical natively unfolded protein, were obtained in the presence and absence of methanol, sodium dodecyl sulfate (SDS), and hexafluoro-2-propanol (HFIP). Consistent with previous CD studies, the secondary structure becomes largely alpha-helical in HFIP and SDS and predominantly beta-sheet in 25% methanol in water. In SDS, an increase in alpha-helical conformation is indicated by the predominant Raman amide I marker band at 1654 cm(-1) and the typical double minimum in the CD spectrum. In 25% HFIP the amide I Raman marker band appears at 1653 cm(-1) with a peak width at half-height of approximately 33 cm(-1), and in 25% methanol the amide I Raman band shifts to 1667 cm(-1) with a peak width at half-height of approximately 26 cm(-1). These well-characterized structural states provide the unequivocal assignment of amide I marker bands in the Raman spectrum of alpha-synuclein and by extrapolation to other natively unfolded proteins. The Raman spectrum of monomeric alpha-synuclein in aqueous solution suggests that the peptide bonds are distributed in both the alpha-helical and extended beta-regions of Ramachandran space. A higher frequency feature of the alpha-synuclein Raman amide I band resembles the Raman amide I band of ionized polyglutamate and polylysine, peptides which adopt a polyproline II helical conformation. Thus, a three-component band fitting is used to characterize the Raman amide I band of alpha-synuclein, phosvitin, alpha-casein, beta-casein, and the non-A beta component (NAC) of Alzheimer's plaque. These analyses demonstrate the ability of Raman spectroscopy to characterize the ensemble of secondary structures present in natively unfolded proteins.
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| pubmed:grant | |
| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Amides,
http://linkedlifedata.com/resource/pubmed/chemical/Amyloid,
http://linkedlifedata.com/resource/pubmed/chemical/Caseins,
http://linkedlifedata.com/resource/pubmed/chemical/Methanol,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Phosvitin,
http://linkedlifedata.com/resource/pubmed/chemical/Propanols,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/SNCA protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Sodium Dodecyl Sulfate,
http://linkedlifedata.com/resource/pubmed/chemical/Solutions,
http://linkedlifedata.com/resource/pubmed/chemical/Synucleins,
http://linkedlifedata.com/resource/pubmed/chemical/alpha-Synuclein,
http://linkedlifedata.com/resource/pubmed/chemical/hexafluoroisopropanol
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| pubmed:status |
MEDLINE
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| pubmed:month |
Mar
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| pubmed:issn |
0002-7863
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:day |
3
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| pubmed:volume |
126
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
2399-408
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| pubmed:dateRevised |
2007-11-14
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| pubmed:meshHeading |
pubmed-meshheading:14982446-Amides,
pubmed-meshheading:14982446-Amino Acid Sequence,
pubmed-meshheading:14982446-Amyloid,
pubmed-meshheading:14982446-Caseins,
pubmed-meshheading:14982446-Circular Dichroism,
pubmed-meshheading:14982446-Humans,
pubmed-meshheading:14982446-Methanol,
pubmed-meshheading:14982446-Molecular Sequence Data,
pubmed-meshheading:14982446-Nerve Tissue Proteins,
pubmed-meshheading:14982446-Phosvitin,
pubmed-meshheading:14982446-Propanols,
pubmed-meshheading:14982446-Protein Conformation,
pubmed-meshheading:14982446-Protein Folding,
pubmed-meshheading:14982446-Protein Structure, Secondary,
pubmed-meshheading:14982446-Recombinant Proteins,
pubmed-meshheading:14982446-Sodium Dodecyl Sulfate,
pubmed-meshheading:14982446-Solutions,
pubmed-meshheading:14982446-Spectrum Analysis, Raman,
pubmed-meshheading:14982446-Synucleins,
pubmed-meshheading:14982446-alpha-Synuclein
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| pubmed:year |
2004
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| pubmed:articleTitle |
Raman spectroscopic characterization of secondary structure in natively unfolded proteins: alpha-synuclein.
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| pubmed:affiliation |
Department of Biochemistry, Case Western Reserve University, Cleveland, Ohio 44106, USA.
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| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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