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Titolo:
DISTRIBUTION OF DISTANCES BETWEEN THE TRYPTOPHAN AND THE N-TERMINAL RESIDUE OF MELITTIN IN ITS COMPLEX WITH CALMODULIN, TROPONIN-C, AND PHOSPHOLIPIDS
Autore:
LAKOWICZ JR; GRYCZYNSKI I; LACZKO G; WICZK W; JOHNSON ML;
Indirizzi:
UNIV MARYLAND,CTR FLUORESCENCE SPECT,SCH MED,DEPT BIOL CHEM,108 N GREENE ST BALTIMORE MD 21201 UNIV VIRGINIA,DEPT PHARMACOL CHARLOTTESVILLE VA 22908
Titolo Testata:
Protein science
fascicolo: 4, volume: 3, anno: 1994,
pagine: 628 - 637
SICI:
0961-8368(1994)3:4<628:DODBTT>2.0.ZU;2-8
Fonte:
ISI
Lingua:
ENG
Soggetto:
FREQUENCY-DOMAIN FLUOROMETRY; FLUORESCENCE ENERGY-TRANSFER; TIME-RESOLVED FLUORESCENCE; LIPID BILAYER MEMBRANES; CHICKEN SKELETAL-MUSCLE; LIGHT-CHAIN KINASE; PHOSPHATIDYLCHOLINE MEMBRANES; CIRCULAR-DICHROISM; ANISOTROPY DECAYS; CRYSTAL-STRUCTURE;
Keywords:
CALMODULIN; DISTANCE DISTRIBUTIONS; FLUORESCENCE SPECTROSCOPY; FREQUENCY-DOMAIN FLUORESCENCE; MELITTIN; PROTEIN CONFORMATION; PROTEIN FOLDING; RESONANCE ENERGY TRANSFER; TROPONIN C;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
71
Recensione:
Indirizzi per estratti:
Citazione:
J.R. Lakowicz et al., "DISTRIBUTION OF DISTANCES BETWEEN THE TRYPTOPHAN AND THE N-TERMINAL RESIDUE OF MELITTIN IN ITS COMPLEX WITH CALMODULIN, TROPONIN-C, AND PHOSPHOLIPIDS", Protein science, 3(4), 1994, pp. 628-637

Abstract

We used frequency-domain measurements of fluorescence resonance energy transfer to measure the distribution of distances between Trp-19 of melittin and a 1-dimethylamino-5-sulfonylnaphthalene (dansyl) residue on the N-terminal-alpha-amino group. Distance distributions were obtained for melittin free in solution and when complexed with calmodulin (CaM), troponin C (TnC), or palmitoyloleoyl-L-alpha-phosphatidylcholine(POPC) vesicles. A wide range of donor (Trp-19)-to-acceptor (dansyl) distances was found for free melittin, which is consistent with that expected for the random coil state, characterized by a Gaussian width (full width at half maxima) of 28.2 Angstrom. In contrast, narrow distance distributions were found for melittin complexed with CaM, 8.2 Angstrom, or with POPC vesicles, 4.9 Angstrom. A somewhat wider distribution was found for the melittin complex with TnC, 12.8 Angstrom, suggesting the presence of heterogeneity in the mode of binding between melittin and TnC. For all the complexes the mean Trp-19 to dansyl distance was near 20 Angstrom. This value is somewhat smaller than expected forthe free alpha-helical state of melittin, suggesting that binding with CaM or TnC results in a modest decrease in the length of the melittin molecule.

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Documento generato il 04/12/20 alle ore 16:16:20