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Structural polymorphism of (1→4)—β—d—Xylan

✍ Scribed by H. Chanzy; M. Dube; R.H. Marchessault


Publisher
Elsevier Science
Year
1979
Tongue
English
Weight
499 KB
Volume
20
Category
Article
ISSN
0032-3861

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The nonbonded interaction energy was computed for xylobiose and xylan as a function of the dihedral angles (+,$). The energy maps indicate that interactions higher than the second neighbor are negligible. Of the four possibilities, the left-handed helical conformation with (+,$) = (63",25") is of th

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## Abstract The enzymatic degradation of β(1 → 4) xylan single crystals with xylanases was investigated by electron microscopy and electron diffraction. The enzyme attack takes place at the edge of the crystals and progresses towards their centers. This is consistent with an __endo__‐enzyme mechani