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Noncovalent Crosslinking of SH1 and SH2 to Detect Dynamic Flexibility of the SH1 Helix

In this experiment, fluorescent N- (1-pyrenyl) iodoacetamide modified the two reactive thiols, SH1 (Cys 707) and SH2 (Cys 697) on myosin to detect SH1-SH2 a -helix melting. The excimer forming property of pyrene is well suited to monitor the dynamics of the SH1 and SH2 helix melting, since the excimer should only form during the melted state. Decreased anisotropy of the excimer relative to the monomeric pyrene fluorescence is consistent with the disordering of the melted SH1-SH2 region in the atomic model. Furthermore, nucleotide analogs induced changes in the anisotropy of the excimer, suggesting that the nucleotide site modulates the flexibility of SH1-SH2 region.

Identiferoai:union.ndltd.org:unt.edu/info:ark/67531/metadc5844
Date08 1900
CreatorsPark, Hyunguk
ContributorsRoot, Douglas D., Donahue, Manus J., Masaracchia, Ruthann A.
PublisherUniversity of North Texas
Source SetsUniversity of North Texas
LanguageEnglish
Detected LanguageEnglish
TypeThesis or Dissertation
FormatText
RightsPublic, Copyright, Park, Hyunguk, Copyright is held by the author, unless otherwise noted. All rights reserved.

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