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218961-09-2

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218961-09-2 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 218961-09-2 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 2,1,8,9,6 and 1 respectively; the second part has 2 digits, 0 and 9 respectively.
Calculate Digit Verification of CAS Registry Number 218961-09:
(8*2)+(7*1)+(6*8)+(5*9)+(4*6)+(3*1)+(2*0)+(1*9)=152
152 % 10 = 2
So 218961-09-2 is a valid CAS Registry Number.

218961-09-2Relevant articles and documents

Regioselective Glycosylation Strategies for the Synthesis of Group Ia and Ib Streptococcus Related Glycans Enable Elucidating Unique Conformations of the Capsular Polysaccharides

Del Bino, Linda,Calloni, Ilaria,Oldrini, Davide,Raso, Maria Michelina,Cuffaro, Rossella,Ardá, Ana,Codée, Jeroen D. C.,Jiménez-Barbero, Jesús,Adamo, Roberto

, p. 16277 - 16287 (2019/11/14)

Group B Streptococcus serotypes Ia and Ib capsular polysaccharides are key targets for vaccine development. In spite of their immunospecifity these polysaccharides share high structural similarity. Both are composed of the same monosaccharide residues and

'Naked' and hydrated conformers of the conserved core pentasaccharide of N-linked glycoproteins and its building blocks

Barry, Conor S.,Cocinero, Emilio J.,Carcabal, Pierre,Gamblin, David P.,Stanca-Kaposta, E. Cristina,Remmert, Sarah M.,Fernandez-Alonso, Maria C.,Rudic, Svemir,Simons, John P.,Davis, Benjamin G.

, p. 16895 - 16903 (2013/12/04)

N-glycosylation of eukaryotic proteins is widespread and vital to survival. The pentasaccharide unit -Man3GlcNAc2- 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-β-1,4-GlcNAc- linkage is more flexible and is modulated by the distal Man-α-1,3- and Man-α-1,6- branching units. Solvation stiffens the 'rod' but leaves the distal residues flexible, through a β-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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