A 1H NMR spectroscopic study on the tryptophan residues of lysozyme included by glucosyl-β-cyclodextrin
T Yamamoto, T Kobayashi, K Yoshikiyo… - Journal of Molecular …, 2009 - Elsevier
A 1H NMR spectroscopic study showed that the side chains of Trp residues of chicken egg
white lysozyme in an aqueous solution are included by Glucosyl-β-cyclodextrin (G1-β-CD).
The 1H NMR signals due to Trp residues shifted with the addition of G1-β-CD. The addition
of methyl α-d-glucopyranoside, which has no inclusion ability, gave different effect on the
shift of 1H NMR signals. The 1H NMR signals due to Cys64 and Ile98 were also influenced
to a considerable extent with the addition of G1-β-CD, suggesting that these hydrophobic …
white lysozyme in an aqueous solution are included by Glucosyl-β-cyclodextrin (G1-β-CD).
The 1H NMR signals due to Trp residues shifted with the addition of G1-β-CD. The addition
of methyl α-d-glucopyranoside, which has no inclusion ability, gave different effect on the
shift of 1H NMR signals. The 1H NMR signals due to Cys64 and Ile98 were also influenced
to a considerable extent with the addition of G1-β-CD, suggesting that these hydrophobic …