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Updated: May 5, 2026
Pull-down of Calmodulin-binding Proteins
Published on: January 23, 2012
Distribution of separations between groups in an engineered calmodulin
R F Steiner1, S Albaugh, M C Kilhoffer
1Department of Chemistry and Biochemistry, University of Maryland (Baltimore County), 5401 Wilkens Avenue, 21228, Baltimore, Maryland.
Abstract:
An engineered calmodulin (VU-9-CaM) has been prepared in which a tryptophan group is present at position 99 and a tyrosine at position 138. The tyrosine was converted to nitrotyrosine. Timedomain dynamic fluorescence measurements were made of energy transfer from the tryptophan donor to the nitrotyrosine acceptor. These were analyzed to yield the parameters characterizing the distribution of separations between the two groups, which are located on Ca(2+)-binding domains III and IV. Their mean separation is in reasonable agreement with the crystallographic value.
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