Fluorescence of native and partially denatured variant-3 scorpion neurotoxin

Christopher Haydock, Salah S. Sedarous, Franklyn G. Prendergast

Research output: Chapter in Book/Report/Conference proceedingConference contribution

Abstract

The multi-component fluorescence intensity decay of variant-3 scorpion neurotoxin is measured with time-correlated single photon counting as a function of guanidine hydrochloride (GuHCl) concentration. Available evidence suggests that while the NH2-terminal β- sheet strand may be denatured in GuHCl, the remaining core neurotoxin structure remains intact. We investigate this hypothesis with computer simulations of variant-3 scorpion neurotoxin with lysine-1 to tyrosine-4 deleted. Previous combination thermodynamic perturbation and umbrella sampling, adiabatic mapping and minimum perturbation mapping computer simulations of tryptophan-47 in the native neurotoxin exhibited multiple rotational isomers that might correspond to the observed fluorescence intensity decay components. The new simulations allow us to compare the number of rotational isomers, the isomer populations, the order parameters, and the transition state theory isomer interconversion rates in the native and denatured states.

Original languageEnglish (US)
Title of host publicationProceedings of SPIE - The International Society for Optical Engineering
Place of PublicationBellingham, WA, United States
PublisherPubl by Int Soc for Optical Engineering
Pages167-171
Number of pages5
Volume1640
ISBN (Print)0819407860
StatePublished - 1992
EventTime-Resolved Laser Spectroscopy in Biochemistry III - Los Angeles, CA, USA
Duration: Jan 20 1992Jan 22 1992

Other

OtherTime-Resolved Laser Spectroscopy in Biochemistry III
CityLos Angeles, CA, USA
Period1/20/921/22/92

Fingerprint

Isomers
isomers
Fluorescence
guanidines
fluorescence
hydrochlorides
computerized simulation
perturbation
lysine
tyrosine
tryptophan
Computer simulation
decay
strands
counting
Photons
sampling
Thermodynamics
Sampling
thermodynamics

ASJC Scopus subject areas

  • Electrical and Electronic Engineering
  • Condensed Matter Physics

Cite this

Haydock, C., Sedarous, S. S., & Prendergast, F. G. (1992). Fluorescence of native and partially denatured variant-3 scorpion neurotoxin. In Proceedings of SPIE - The International Society for Optical Engineering (Vol. 1640, pp. 167-171). Bellingham, WA, United States: Publ by Int Soc for Optical Engineering.

Fluorescence of native and partially denatured variant-3 scorpion neurotoxin. / Haydock, Christopher; Sedarous, Salah S.; Prendergast, Franklyn G.

Proceedings of SPIE - The International Society for Optical Engineering. Vol. 1640 Bellingham, WA, United States : Publ by Int Soc for Optical Engineering, 1992. p. 167-171.

Research output: Chapter in Book/Report/Conference proceedingConference contribution

Haydock, C, Sedarous, SS & Prendergast, FG 1992, Fluorescence of native and partially denatured variant-3 scorpion neurotoxin. in Proceedings of SPIE - The International Society for Optical Engineering. vol. 1640, Publ by Int Soc for Optical Engineering, Bellingham, WA, United States, pp. 167-171, Time-Resolved Laser Spectroscopy in Biochemistry III, Los Angeles, CA, USA, 1/20/92.
Haydock C, Sedarous SS, Prendergast FG. Fluorescence of native and partially denatured variant-3 scorpion neurotoxin. In Proceedings of SPIE - The International Society for Optical Engineering. Vol. 1640. Bellingham, WA, United States: Publ by Int Soc for Optical Engineering. 1992. p. 167-171
Haydock, Christopher ; Sedarous, Salah S. ; Prendergast, Franklyn G. / Fluorescence of native and partially denatured variant-3 scorpion neurotoxin. Proceedings of SPIE - The International Society for Optical Engineering. Vol. 1640 Bellingham, WA, United States : Publ by Int Soc for Optical Engineering, 1992. pp. 167-171
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