Linked Life Data

1924399

Source:http://linkedlifedata.com/resource/pubmed/id/1924399

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
20
pubmed:dateCreated
1991-11-15
pubmed:abstractText
The solution conformation behavior of complex oligosaccharides was studied by resonance energy transfer, as measured by the time-resolved fluorescence method, to determine the conformational heterogeneity of a triantennary glycopeptide at various temperatures. Groups that acted as a fluorescence donor (naphthyl-2-acetyl, Nap) or acceptor (dansylethylenediamine, Dan) were selectively attached to the N terminus of the peptide and a Gal residue [either 6' (shown below), 6, or 8] of the oligosaccharide, respectively. [formula: see text] Time-resolved fluorescence energy-transfer measurements revealed two populations of conformers when Dan was attached to either Gal-6' or Gal-6. One conformer contained the antenna folded back toward the core region, and a second was in an extended conformation. The two conformations differed in donor-acceptor distance by about 10 A. Systematically increasing the temperature from 0 degrees C to 40 degrees C increased the ratio of extended to folded forms 2-fold for the Gal-6 isomer and 4-fold for the Gal-6' isomer, whereas the Gal-8 isomer showed only a single distance population throughout this temperature range. From these data, delta H and delta S for the reversible conformational change were calculated to be 3.1 kcal/mol and 10.8 cal/(mol.K) for the Gal-6 isomer and 7.1 kcal/mol and 25.8 cal/(mol.K) for the Gal-6' isomer. In addition to the structural microheterogeneity commonly associated with glycoproteins, the differential flexibilities of the different branches in the oligosaccharides contribute conformational heterogeneity and should be considered in conformational analysis. The data are discussed in terms of the most probable linkages that contribute to the observed flexibility of the individual triantennary branches, and the biological significance of flexible linkages in complex carbohydrates is considered.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/1924399-1057171, http://linkedlifedata.com/resource/pubmed/commentcorrection/1924399-2065052, http://linkedlifedata.com/resource/pubmed/commentcorrection/1924399-2211710, http://linkedlifedata.com/resource/pubmed/commentcorrection/1924399-2211711, http://linkedlifedata.com/resource/pubmed/commentcorrection/1924399-2328229, http://linkedlifedata.com/resource/pubmed/commentcorrection/1924399-2386786, http://linkedlifedata.com/resource/pubmed/commentcorrection/1924399-3052290, http://linkedlifedata.com/resource/pubmed/commentcorrection/1924399-3322384, http://linkedlifedata.com/resource/pubmed/commentcorrection/1924399-3427034, http://linkedlifedata.com/resource/pubmed/commentcorrection/1924399-3896128, http://linkedlifedata.com/resource/pubmed/commentcorrection/1924399-481233, http://linkedlifedata.com/resource/pubmed/commentcorrection/1924399-6262134, http://linkedlifedata.com/resource/pubmed/commentcorrection/1924399-6825693
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0027-8424
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
88
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
9355-9
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
Differential flexibilities in three branches of an N-linked triantennary glycopeptide.
pubmed:affiliation
Department of Biology, Johns Hopkins University, Baltimore, MD 21218.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S.