Intensity and anisotropy decays of the tyrosine calmodulin proteolytic fragments, as studied by GHz frequency-domain fluorescence

I. Gryczynski, R. F. Steiner, J. R. Lakowicz

Research output: Contribution to journalArticle

21 Scopus citations

Abstract

Frequency-domain fluorescence measurements to 2 GHz were able to recover and account for essentially all of the intrinsic tyrosine anisotropy of calmodulin and its proteolytic fragments containing one or two tyrosine residues. Low-temperature measurements have detected a very rapid initial anisotropy decay in the 2-tyrosine species which may be attributed to radiationless energy transfer between the two tyrosines. The observed values of the rotational correlation times indicate that both tyrosines of calmodulin possess considerable mobility, which decreases in the presence of Ca2+ and at low temperatures.

Original languageEnglish
Pages (from-to)69-78
Number of pages10
JournalBiophysical Chemistry
Volume39
Issue number1
DOIs
StatePublished - Jan 1991

Keywords

  • Anisotropy
  • Ca
  • Calmodulin
  • Energy transfer
  • Fluorescence
  • Protein dynamics
  • Tyrosine

Fingerprint Dive into the research topics of 'Intensity and anisotropy decays of the tyrosine calmodulin proteolytic fragments, as studied by GHz frequency-domain fluorescence'. Together they form a unique fingerprint.

  • Cite this