Abstract
We report the first anisotropy decays of protein fluorescence obtained using a frequency-domain fluorometer. The ultraviolet light source (300 nm) was a ring dye laser equipped with an intracavity frequency doubler, pumped by an argon ion laser. The data, measured at modulation frequencies from 2 to 200 MHz, reveal the presence of subnanosecond motions (0.1-0.2 ns) of the single tryptophan residues in melittin and monellin. For melittin the data also indicate the presence of slower motions near 1 ns, which may be the result of concerted motions of several peptide units. Smaller amplitude motions, on a similar timescale, were observed for the single tryptophan residue in staphylococcal nuclease. We demonstrate using N-acetyl-L-tryptophanamide in water that the method of frequency-domain fluorometry is capable of measuring correlation times as short as 50 ps. This method can provide data for the direct comparison of measured anisotropy decays with those prediced from molecular dynamics calculations.
| Original language | English |
|---|---|
| Pages (from-to) | 2240-2245 |
| Number of pages | 6 |
| Journal | Journal of Biological Chemistry |
| Volume | 261 |
| Issue number | 5 |
| State | Published - 1 Dec 1986 |
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Measurement of subnanosecond anisotropy decays of protein fluorescence using frequency-domain fluorometry. / Lakowicz, J. R.; Laczko, G.; Gryczynski, Ignacy; Cherek, H.
In: Journal of Biological Chemistry, Vol. 261, No. 5, 01.12.1986, p. 2240-2245.Research output: Contribution to journal › Article
TY - JOUR
T1 - Measurement of subnanosecond anisotropy decays of protein fluorescence using frequency-domain fluorometry
AU - Lakowicz, J. R.
AU - Laczko, G.
AU - Gryczynski, Ignacy
AU - Cherek, H.
PY - 1986/12/1
Y1 - 1986/12/1
N2 - We report the first anisotropy decays of protein fluorescence obtained using a frequency-domain fluorometer. The ultraviolet light source (300 nm) was a ring dye laser equipped with an intracavity frequency doubler, pumped by an argon ion laser. The data, measured at modulation frequencies from 2 to 200 MHz, reveal the presence of subnanosecond motions (0.1-0.2 ns) of the single tryptophan residues in melittin and monellin. For melittin the data also indicate the presence of slower motions near 1 ns, which may be the result of concerted motions of several peptide units. Smaller amplitude motions, on a similar timescale, were observed for the single tryptophan residue in staphylococcal nuclease. We demonstrate using N-acetyl-L-tryptophanamide in water that the method of frequency-domain fluorometry is capable of measuring correlation times as short as 50 ps. This method can provide data for the direct comparison of measured anisotropy decays with those prediced from molecular dynamics calculations.
AB - We report the first anisotropy decays of protein fluorescence obtained using a frequency-domain fluorometer. The ultraviolet light source (300 nm) was a ring dye laser equipped with an intracavity frequency doubler, pumped by an argon ion laser. The data, measured at modulation frequencies from 2 to 200 MHz, reveal the presence of subnanosecond motions (0.1-0.2 ns) of the single tryptophan residues in melittin and monellin. For melittin the data also indicate the presence of slower motions near 1 ns, which may be the result of concerted motions of several peptide units. Smaller amplitude motions, on a similar timescale, were observed for the single tryptophan residue in staphylococcal nuclease. We demonstrate using N-acetyl-L-tryptophanamide in water that the method of frequency-domain fluorometry is capable of measuring correlation times as short as 50 ps. This method can provide data for the direct comparison of measured anisotropy decays with those prediced from molecular dynamics calculations.
UR - http://www.scopus.com/inward/record.url?scp=0022969398&partnerID=8YFLogxK
M3 - Article
C2 - 3944133
AN - SCOPUS:0022969398
VL - 261
SP - 2240
EP - 2245
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 5
ER -