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Titolo: INTRAMOLECULAR DYNAMICS IN THE ENVIRONMENT OF THE SINGLE TRYPTOPHAN RESIDUE IN STAPHYLOCOCCAL NUCLEASE
Autore: DEMCHENKO AP; GRYCZYNSKI I; GRYCZYNSKI Z; WICZK W; MALAK H; FISHMAN M;
- Indirizzi:
- UNIV MARYLAND,SCH MED,CTR FLUORESCENCE SPECT,DEPT BIOCHEM,108 N GREENE ST BALTIMORE MD 21201 UNIV MARYLAND,SCH MED,CTR FLUORESCENCE SPECTROSCOPY,DEPT BIOCHEM BALTIMORE MD 21201 AV PALLADIN BIOCHEM INST KIEV 252030 UKRAINE
- Titolo Testata:
- Biophysical chemistry
fascicolo: 1,
volume: 48,
anno: 1993,
pagine: 39 - 48
- SICI:
- 0301-4622(1993)48:1<39:IDITEO>2.0.ZU;2-N
- Fonte:
- ISI
- Lingua:
- ENG
- Soggetto:
- FLUORESCENCE EMISSION-SPECTRA; PHASE-MODULATION FLUOROMETRY; VARIABLE-FREQUENCY PHASE; RED-EDGE-EXCITATION; PROTEIN DYNAMICS; SPECTROSCOPY; WATER; ANISOTROPIES; HYDRATION; STABILITY;
- Keywords:
- TRYPTOPHAN; INTRAMOLECULAR DYNAMICS; STAPHYLOCOCCAL NUCLEASE; TIME-RESOLVED FLUORESCENCE;
- Tipo documento:
- Article
- Natura:
- Periodico
- Settore Disciplinare:
- Science Citation Index Expanded
- Science Citation Index Expanded
- Science Citation Index Expanded
- Citazioni:
- 43
- Recensione:
- Indirizzi per estratti:
-
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- Citazione:
- A.P. Demchenko et al., "INTRAMOLECULAR DYNAMICS IN THE ENVIRONMENT OF THE SINGLE TRYPTOPHAN RESIDUE IN STAPHYLOCOCCAL NUCLEASE", Biophysical chemistry, 48(1), 1993, pp. 39-48
Abstract
The dipole relaxational dynamics in the environment of a single tryptophan residue Trp-140 in staphylococcal nuclease was studied by time-resolved (multi-frequency phase-modulation) spectroscopy and selective red-edge excitation. The long-wavelength position of the fluorescence spectrum (at 343 nm) and the absence of red-edge excitation effects at0 and 20 degrees C indicate that this residue is surrounded by very mobile protein groups which relax on the subnanosecond time scale. For these temperatures (0-20 degrees C) the steady-state emission spectra did not show the excitation-wavelength dependent shifts (red-edge effects) for excitation wavelengths from 295 to 308 nm; however, the anisotropy decay rate is slow (tens of nanoseconds). This suggests that thespectral relaxation is due to mobility of the surrounding groups rather than :he motion of the tryptophan itself. The motions of the tryptophan surrounding are substantially retarded at reduced temperatures inviscous solvent (60% glycerol). The temperature dependence of the difference in position of fluorescence spectra at excitation wavelengths 295 and 305 nm demonstrate the existence of red-edge effect at sub-zero temperatures, reaching a maximum value at - 50 degrees C, where the steady-state emission spectrum is shifted to 332 nm. The excitation and emission wavelength dependence of multi-frequency phase-modulation data at the half-transition point (-40 degrees C) demonstrates the existence of the nanosecond dipolar relaxations. At - 40 degrees C the time-dependent spectral shift is close to monoexponential with the relaxation time of 1.4 ns.
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Documento generato il 04/12/20 alle ore 16:44:01