Conformational influences of glycosylation of a peptide: A possible model for the effect of glycosylation on the rate of protein folding Journal Article

   


Authors: Live, D. H.; Kumar, R. A.; Beebe, X.; Danishefsky, S. J.
Article Title: Conformational influences of glycosylation of a peptide: A possible model for the effect of glycosylation on the rate of protein folding
Abstract: Improved strategies for synthesis make it possible to expand the range of glycopeptides available for detailed conformational studies. The glycopeptide 1 was synthesized using a new solid phase synthesis of carbohydrates and a convergent coupling to peptide followed by deprotection. Its conformational properties were subjected to NMR analysis and compared with a control peptide 2 prepared by conventional solid phase methods. Whereas peptide 2 fails to manifest any appreciable secondary structure, the glycopeptide 1 does show considerable conformational bias suggestive of an equilibrium between an ordered and a random state. The implications of this ordering effect for the larger issue of protein folding are considered.
Keywords: conference paper; protein conformation; protein binding; molecular sequence data; glycosylation; magnetic resonance spectroscopy; models, molecular; conformational transition; protein folding; protein secondary structure; glycoproteins; protein structure, secondary; nuclear magnetic resonance; carbohydrate sequence; glycopeptide; glycopeptides; carbohydrate conformation; peptide analysis; protein glycosylation; priority journal
Journal Title: Proceedings of the National Academy of Sciences of the United States of America
Volume: 93
Issue: 23
ISSN: 0027-8424
Publisher: National Academy of Sciences  
Date Published: 1996-11-12
Start Page: 12759
End Page: 12761
Language: English
DOI: 10.1073/pnas.93.23.12759
PUBMED: 8917491
PROVIDER: scopus
PMCID: PMC23992
DOI/URL:

https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029803424&doi=10.1073%2fpnas.93.23.12759&partnerID=40&md5=81458c89dfbd2cdd157349418ac415b0
Notes: Conference Paper -- Export Date: 22 November 2017 -- Source: Scopus
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MSK Authors
  1. Samuel J Danishefsky
    539 Danishefsky
  2. Rakesh Ajay Kumar
    12 Kumar
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