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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1-3
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pubmed:dateCreated |
2003-1-31
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pubmed:abstractText |
A set of designed internally quenched fluorescence peptide substrates has been used to probe the effects of insertion of beta-peptide bonds into peptide sequences. The test sequence chosen corresponds to a proteolytically susceptible site in hemoglobin alpha-chain, residues 32-37. Fluorescence and mass spectral measurements demonstrate that the insertion of an beta-residues at the potential cleavage sites completely abolishes the action of proteases; in addition, the rate of cleavage of the peptide bond preceding the site of modification is also considerably reduced.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/1,5-I-AEDANS,
http://linkedlifedata.com/resource/pubmed/chemical/4-(4-dimethylaminophenylazo)benzoic...,
http://linkedlifedata.com/resource/pubmed/chemical/Aspartic Acid Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Chymotrypsin,
http://linkedlifedata.com/resource/pubmed/chemical/Endopeptidase K,
http://linkedlifedata.com/resource/pubmed/chemical/Fluorescent Dyes,
http://linkedlifedata.com/resource/pubmed/chemical/Hemoglobins,
http://linkedlifedata.com/resource/pubmed/chemical/Naphthalenesulfonates,
http://linkedlifedata.com/resource/pubmed/chemical/Pepsin A,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Protozoan Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Trypsin,
http://linkedlifedata.com/resource/pubmed/chemical/p-Dimethylaminoazobenzene,
http://linkedlifedata.com/resource/pubmed/chemical/plasmepsin II
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0014-5793
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
30
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pubmed:volume |
535
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
175-8
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:12560099-Animals,
pubmed-meshheading:12560099-Aspartic Acid Endopeptidases,
pubmed-meshheading:12560099-Binding Sites,
pubmed-meshheading:12560099-Chymotrypsin,
pubmed-meshheading:12560099-Endopeptidase K,
pubmed-meshheading:12560099-Fluorescent Dyes,
pubmed-meshheading:12560099-Hemoglobins,
pubmed-meshheading:12560099-Naphthalenesulfonates,
pubmed-meshheading:12560099-Pepsin A,
pubmed-meshheading:12560099-Peptides,
pubmed-meshheading:12560099-Plasmodium falciparum,
pubmed-meshheading:12560099-Protozoan Proteins,
pubmed-meshheading:12560099-Spectrometry, Fluorescence,
pubmed-meshheading:12560099-Spectrometry, Mass, Matrix-Assisted Laser...,
pubmed-meshheading:12560099-Substrate Specificity,
pubmed-meshheading:12560099-Trypsin,
pubmed-meshheading:12560099-p-Dimethylaminoazobenzene
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pubmed:year |
2003
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pubmed:articleTitle |
Proteolytic stability of beta-peptide bonds probed using quenched fluorescent substrates incorporating a hemoglobin cleavage site.
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pubmed:affiliation |
Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560 012, India.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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