Journal
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 135, Issue 45, Pages 16895-16903Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ja4056678
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Funding
- Leverhulme Trust
- Royal Society
- Wolfson Foundation
- EPSRC
- Spanish Ministry (MICINN) [CTQ2011-22923]
- SGIker at UPV-EHU
- Triangle de la Physique [2010-079T]
- BBSRC [BB/E004350/1] Funding Source: UKRI
- EPSRC [EP/E000614/1, EP/I500200/1, EP/G026688/1, EP/G03088X/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [EGA17763, BB/C510824/1, BB/E004350/1] Funding Source: researchfish
- Engineering and Physical Sciences Research Council [EP/E000614/1, EP/D023335/1, GR/T26542/01, EP/D023343/1, EP/I500200/1, EP/G03088X/1, EP/G026688/1] Funding Source: researchfish
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N-glycosylation of eukaryotic proteins is widespread and vital to survival. The pentasaccharide unit -Man(3)GlcNAc(2)- lies at the protein-junction core of all oligosaccharides attached to asparagine side chains during this process. Although its absolute conservation implies an indispensable role, associated perhaps with its structure, its unbiased conformation and the potential modulating role of solvation are unknown; both have now been explored through a combination of synthesis, laser spectroscopy, and computation. The proximal -GlcNAc-GlcNAc- unit acts as a rigid rod, while the central, and unusual, -Man-beta-1,4-GlcNAc- linkage is more flexible and is modulated by the distal Man-alpha-1,3- and Man-alpha-1,6- branching units. Solvation stiffens the 'rod' but leaves the distal residues flexible, through a beta-Man pivot, ensuring anchored projection from the protein shell while allowing flexible interaction of the distal portion of N-glycosylation with bulk water and biomolecular assemblies.
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