2012
DOI: 10.1007/s10867-012-9280-x
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Folding of pig gastric mucin non-glycosylated domains: a discrete molecular dynamics study

Abstract: Mucin glycoproteins consist of tandem-repeating glycosylated regions flanked by non-repetitive protein domains with little glycosylation. These non-repetitive domains are involved in polymerization of mucin and play an important role in the pH-dependent gelation of gastric mucin, which is essential for protecting the stomach from autodigestion. We examine folding of the non-repetitive sequence of PGM-2X (242 amino acids) and the von Willebrand factor vWF-C1 domain (67 amino acids) at neutral and low pH using d… Show more

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Cited by 18 publications
(23 citation statements)
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“…SASA per residue values reflect structural conformational changes at protein surfaces; lower values mean residues are buried inside globular folded conformations [37][38][39] . This analysis together and the RMSF study suggest that the Y38C, W50C, T66M, and V126G increase solvent exposure, modulate protein-protein interactions, and possibly increase aggregation propensity [40][41][42] . Figure 2.…”
Section: Resultsmentioning
confidence: 67%
“…SASA per residue values reflect structural conformational changes at protein surfaces; lower values mean residues are buried inside globular folded conformations [37][38][39] . This analysis together and the RMSF study suggest that the Y38C, W50C, T66M, and V126G increase solvent exposure, modulate protein-protein interactions, and possibly increase aggregation propensity [40][41][42] . Figure 2.…”
Section: Resultsmentioning
confidence: 67%
“…This conclusion is consistent with previous reports that ionic interactions underlie the effect of pH on mucus viscosity (47,49). However, the variations in pH might also affect H + bonds and salt bridges, and hydrophobic interactions have been observed at very low pH values (77). Sites on mucus that might contribute to electrostatic interactions include the mucin protein backbone (especially the N-and C-terminal ends) and negatively charged sulfate or sialic acid on O-glycan structures.…”
Section: Discussionmentioning
confidence: 99%
“…implemented amino acid‐specific interactions due to hydropathy and charge into the four‐bead model, which define the DMD4B‐HYDRA force field . The specificity of hydropathic interactions is based on the generic Kyte‐Doolittle hydropathy scale, which makes the DMD4B‐HYDRA approach broadly applicable to studies of protein folding and assembly ,,…”
Section: Mysterious Aβ Oligomersmentioning
confidence: 99%