• Title/Summary/Keyword: sidechains

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Changes in Solution Properties of Pectins by Enzymatic Hydrolysis of Sidechains

  • Hwang, Jae-Kwan;Jozef L. Kokini
    • Journal of the Korean Society of Food Science and Nutrition
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    • v.24 no.3
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    • pp.389-395
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    • 1995
  • The neutral sugar sidechains of apple pectins were hydrolyzed by commercial hemicellulase produced from Aspergillus niger, and the corresponding changes in solution viscosity were investigated in dilute(cc*) pectin solutions. Pectinase activity included in hemicellulases was removed by Epoxy-activated Sepharose 6B affinity chromatography using polygalacturonic acid as a ligand. Enzymatic hydrolysis of sidechains did not affect the specifc viscosity of dilute(0.5%) pectin solutions, while viscosity significantly decreased in concentrated(2.0∼6.0%) region. These results strongly suggest that the sidechains of pectins exists as an entangled state in concentrated solutions. It was also found that in the concentrated region the extent of viscosity reduction was dependent on pectin concentrations.

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Transverse relaxation-optimized HCN experiment for tautomeric states of histidine sidechains

  • Schmidt, Holger;Himmel, Sebastian;Walter, Korvin F.A.;Klaukien, Volker;Funk, Michael;Lee, Dong-Han
    • Journal of the Korean Magnetic Resonance Society
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    • v.12 no.2
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    • pp.89-95
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    • 2008
  • Function of protein is frequently related with tautomeric states of histidine sidechains. Thus, several NMR experiments were developed to determine the tautomeric states of histidines. However, poor sensitivity of these experiments caused by long duration of magnetization transfer periods is unavoidable. Here, we alleviate the sensitivity of HCN experiment for determining the tautomeric states of histidine residues using TROSY principle to suppress transverse relaxation of $^{13}C$ spins during long polarization transfer delays involving $^{13}C-^{15}N$ scalar couplings. In addition, this experiment was used to assign the sidechain resonances of histidines. These assignments can be used to follow the pH-titration of histidine sidechains.

The Solid-Phase Synthesis of Amino Acid-Derived Diacetylene Lipids

  • Kim Jong-Man;Park Bum Jun;Chang Eun-Ju;Yi Sung Chul;Suh Dong Hack;Ahn Dong June
    • Macromolecular Research
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    • v.13 no.3
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    • pp.253-256
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    • 2005
  • We prepared amino acid-derived diacetylene monomers using solid-phase organic synthesis. The solid-phase synthetic method allowed for the rapid and efficient preparation of functional diacetylenes. Amino acids having hydrophobic sidechains such as alanine, leucine, and phenylalanine, as well as hydrophilic sidechains such as aspartic acid and lysine, were successfully coupled to the diacetylene lipid. The diacetylene monomers prepared in this way were subjected to routine procedures for the generation of polydiacetylene vesicles. Depending on the nature of the side-chains, pink to blue colored polydiacetylenes were generated.