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Author Liu X.Q., Zhang D., Zhang X.M., Wang C.T., Liu X.Q., Tan Y.P., Wu Y.H.
Title Study on the interaction between methyl jasmonate and the coiled-coil domain of rice blast resistance protein Pi36 by spectroscopic methods.
Abstract:
Interaction between the coiled-coil domain of rice blast resistance protein Pi36 and methyl-jasmonate (MeJA) was studied by fluorescence and UV-vis spectroscopic techniques. The quenching mechanism of fluorescence of MeJA by this domain was discussed to be a static quenching procedure. Fluorescence quenching was explored to measure the number of binding sites n and apparent binding constants K. The thermodynamics parameters DeltaH, DeltaG, DeltaS were also calculated. The results indicate the binding reaction was not entropy-driven but enthalpy-driven, and hydrophobic binding played major role in the interaction. The binding sites of MeJA with the coiled-coil structural domain of rice blast resistance protein Pi36 were found to approach the microenvironment of both Tyr and Trp by the synchronous fluorescence spectrometry. The distance r between donor (the coiled-coil domain of rice blast resistance protein Pi36) and acceptor (MeJA) was obtained according to Fテカrster theory of non-radioactive energy transfer.
Journal Spectrochim Acta A Mol Biomol Spectrosc
Country China
Volume 88
Pages 72-6
Year 2012
PubMed ID 22196797
PubMed Central ID -
DOI -
URL -
Relation
Gene PI36
INSD -
Strain Wild Core Collection -
Induced Mutation Lines(NIG Collection) -
Sterile Seed Strain -
Lethal Embryo
Mutantion Strain
-
Stages in Each Organ
- Muant Lines (Gene)
-
Cultivated Varieties(NIG Collection) -
Stages in Each Organ -
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