Title : Structural studies on the bacterial cell wall peptidoglycan pseudomurein. I. Conformational energy calculations on the glycan strands in C1 conformation and comparison with murein.

Pub. Date : 1984 Mar 7

PMID : 6547193






4 Functional Relationships(s)
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1 Both types of polysaccharides poly-(NAG-NAT) considered in this study favoured extended conformations, which in the case of 1,3 linked polymers showed less gain of length per saccharide unit compared to 1,4 linked poly-(NAG-NAT) residues. Polysaccharides N-acetyl-alpha-glucosaminidase Homo sapiens
2 Both types of polysaccharides poly-(NAG-NAT) considered in this study favoured extended conformations, which in the case of 1,3 linked polymers showed less gain of length per saccharide unit compared to 1,4 linked poly-(NAG-NAT) residues. Polysaccharides N-acetyl-alpha-glucosaminidase Homo sapiens
3 For a 1,3 linked sugar moiety of pseudomurein every pair of neighbouring peptides attached to glycan chain pointed in favoured conformations approximately to opposite sides of the strands, whereas in a 1,4 linked poly-(NAG-NAT) the peptides protruded approximately to the same side of the glycan moiety. Polysaccharides N-acetyl-alpha-glucosaminidase Homo sapiens
4 In poly-(1,3-NAG-NAT) the glycan chains possessed a zig-zag-like arrangement, whereas for glycan chains of the murein type relatively flat structures were preferred. Polysaccharides N-acetyl-alpha-glucosaminidase Homo sapiens