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NMR processing:
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Side-chains:
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Ab initio:
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Fragment-based:
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Template-based:
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Refinement:
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Structure from chemical shifts:
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Secondary structure from chemical shifts:
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Flexibility from chemical shifts:
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Chemical shifts re-referencing:
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From sequence:
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Disordered proteins:
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Format conversion & validation:
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From NMR-STAR 3.1
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NMR sample preparation:
Protein disorder:
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Protein solubility:
camLILA
ccSOL
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Isotope labeling:
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Solid-state NMR:
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Old 11-19-2010, 08:32 PM
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Default NMR and molecular modeling of complex carbohydrates and carbohydrate-protein interact

NMR and molecular modeling of complex carbohydrates and carbohydrate-protein interactions. Applications to anti-bacteria vaccines.

Related Articles NMR and molecular modeling of complex carbohydrates and carbohydrate-protein interactions. Applications to anti-bacteria vaccines.

Adv Exp Med Biol. 2001;491:543-50

Authors: Brisson JR, Jennings HJ

In order to characterize the conformational epitope of the group B meningococcal polysaccharide and of the type III group B Streptococcus capsular polysaccharide NMR measurements were done on a wide variety of native and modified polysaccharides and oligosaccharides. Since these saccharides are highly mobile and exist as random coils in solution, the analysis of the NMR data and molecular modeling was done to take into account this inherent flexibility. The conformational model of extended high-order helices being selected upon binding to a protein, although still hypothetical at this stage, has proven useful in explaining the serology for the conformational epitopes for polysaccharides of group B Neisseria meningitidis, group B Streptococcus type III and Streptococcus pneumoniae type 14.

PMID: 14533821 [PubMed - indexed for MEDLINE]



Source: PubMed
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