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Distribution of N-glycosylation sequons in proteins: How apart are they?

Paper ID Volume ID Publish Year Pages File Format Full-Text
15230 1394 2011 5 PDF Available
Title
Distribution of N-glycosylation sequons in proteins: How apart are they?
Abstract

N-glycosylation is a common protein modification process, which affects a number of properties of proteins. Little is known about the distribution of N-glycosylation sequons, for example, the distance between glycosylated sites and their position in the protein primary sequence. Using a large set of experimentally confirmed eukaryotic N-glycoproteins we analyzed the relative position and distribution of sequons. N-Glycosylation probability was found to be lower in the termini of protein sequences compared to the mid region. N-glycosylated sequons were found much farther from C terminus compared to the N-terminus of the protein sequence and this effect was more pronounced for NXS sequons. The distribution of sequons, modeled based on balls-in-boxes classical occupancy, showed a near-maximum probability. Considerable proportion of sequons was found within a distance of ten amino acids, indicating that the steric hindrance was not a key factor in protein N-glycosylation. Interestingly, the distribution of all sequons present in N-glycoproteins showed a pattern very similar to that of glycosylated sequons. The results indicate that protein N-glycosylation chiefly follows a random design.

Graphical abstractFigure optionsDownload full-size imageDownload as PowerPoint slideResearch highlights► Probability of sequons and N-glycosylation is low at termini of protein sequences. ► Distribution probability of sequons is close to theoretical maximum. ► Steric hindrance may not be a chief factor in protein N-glycosylation. ► Protein N-glycosylation chiefly follows a random design.

Keywords
Distribution; N-glycoprotein; Probability; Randomness; Sequon
First Page Preview
Distribution of N-glycosylation sequons in proteins: How apart are they?
Publisher
Database: Elsevier - ScienceDirect
Journal: Computational Biology and Chemistry - Volume 35, Issue 2, April 2011, Pages 57–61
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering