Picosecond fluorescence decay of tryptophans in myoglobin
about
Steady-state and time-resolved fluorescence studies on wild type and mutant chromatium vinosum high potential iron proteins: holo- and apo-forms.Femtosecond dynamics of rubredoxin: tryptophan solvation and resonance energy transfer in the protein.Absorption spectra indicate conformational alteration of myoglobin adsorbed on polydimethylsiloxaneHeme-protein interactions in horse heart myoglobin at neutral pH and exposed to acid investigated by time-resolved fluorescence in the pico- to nanosecond time range.Ultrafast tryptophan-to-heme electron transfer in myoglobins revealed by UV 2D spectroscopy.Binding of 7-methoxy-4-(aminomethyl)-coumarin to wild-type and W128F mutant cytochrome P450 2D6 studied by time-resolved fluorescence spectroscopyEffect of disordered hemes on energy transfer rates between tryptophans and heme in myoglobin.Molecular dynamics simulations of oxidized and reduced Clostridium beijerinckii flavodoxin.Resolution of the fluorescence decay of the two tryptophan residues of lac repressor using single tryptophan mutantsFluorescence quenching dynamics of tryptophan in proteins. Effect of internal rotation under potential barrierFluorescence and energy transfer of tryptophans in Aplysia myoglobin.Tryptophan sidechain dynamics in hydrophobic oligopeptides determined by use of 13C nuclear magnetic resonance spectroscopy.Molecular dynamics simulations of fluorescence polarization of tryptophans in myoglobin.Tryptophan-to-heme electron transfer in ferrous myoglobinsApplications of ultrafast laser spectroscopy for the study of biological systems.Temperature-dependent heme kinetics with nonexponential binding and barrier relaxation in the absence of protein conformational substates.Investigations of vibrational coherence in the low-frequency region of ferric heme proteins.A fluorescence decay time study of tryptophan in isolated hemoglobin subunits.Protein dynamics: comparison of simulations with inelastic neutron scattering experiments.Functional electric field changes in photoactivated proteins revealed by ultrafast Stark spectroscopy of the Trp residues.The use of fluorescence methods to monitor unfolding transitions in proteins.Decay of the tryptophan fluorescence anisotropy in bacteriorhodopsin and its modified forms.Ligand-dependent conformational equilibria of serum albumin revealed by tryptophan fluorescence quenching.Heme protein fluorescence versus pressure.A model for multiexponential tryptophan fluorescence intensity decay in proteins.Chemistry. FRETting over the spectroscopic ruler.Hemin and bile pigments are the secondary structure regulators of intrinsically disordered antimicrobial peptides.Charge migration and charge transfer in molecular systems.
P2860
Q28359673-C5C0A027-E6AF-4E24-9D3C-AAB169E070AFQ30329283-AA851920-192C-4CF2-A5D2-42ACA1A212BBQ30417425-8245BFF2-4C12-477D-92ED-B47971519D65Q30417559-AF297A9E-05CB-4B8D-9C75-7FE9128C9DC9Q30426937-4129FB82-7106-41B2-9B10-711EE1D134E0Q33224153-BE538D26-F570-4133-8BCE-23F997AF0037Q34019999-DD867BC7-A908-4070-B807-DBAD8844F5C0Q34114952-B5679502-0A2B-420F-A8F3-3EBEE819FCB0Q34126299-A2BB8D29-8F40-4615-ABF0-1B93F4620564Q34259066-AF2DD3A1-D608-4A1F-9884-06C3BBF4EB0DQ34259142-BE87D8EA-7A08-4E69-BD90-1DE3BC151A30Q34260492-4619288B-4E7B-4645-B1DF-D48B04E503ABQ34342691-AC1CB6B8-6835-4891-9372-17950D9B3FEDQ35590292-64858D88-4942-4F10-9082-724CA9493361Q35951110-3ED11694-25E0-42CF-A843-2A93FB987D5DQ35990258-FCB5B45D-C346-41AF-A511-01FC35927959Q36481531-F8D0CBC5-708F-499F-BC0E-3FCACB08E4C2Q36494243-1B1247F0-1C3F-4F35-8756-FE7FB44F02ADQ36820082-D4A9880E-8200-4626-A77F-1107E330CAD5Q37194751-E730661B-A702-4BF6-BF92-9667D2A0F391Q39454755-309B154C-E88C-444C-A398-629147D79361Q39627248-6D234D10-56DD-4E31-A5EF-F93D6608297CQ40141326-0C3BF7F4-7C9C-46C2-AB1D-CF6649E1B4E2Q41144290-10A315D9-4F32-4D88-9249-7A546F6BB77DQ43006243-043C5B4A-749F-4161-B89F-7ACFC11A1938Q45181621-98AD0711-28C6-4ECC-B626-B7616CB6684DQ47432953-AD1874E4-F4FD-4E26-BE70-6420AEDFDEACQ49776983-DFB1621A-EE07-40BC-A269-D827131773CF
P2860
Picosecond fluorescence decay of tryptophans in myoglobin
description
1984 nî lūn-bûn
@nan
1984年の論文
@ja
1984年学术文章
@wuu
1984年学术文章
@zh-cn
1984年学术文章
@zh-hans
1984年学术文章
@zh-my
1984年学术文章
@zh-sg
1984年學術文章
@yue
1984年學術文章
@zh
1984年學術文章
@zh-hant
name
Picosecond fluorescence decay of tryptophans in myoglobin
@ast
Picosecond fluorescence decay of tryptophans in myoglobin
@en
type
label
Picosecond fluorescence decay of tryptophans in myoglobin
@ast
Picosecond fluorescence decay of tryptophans in myoglobin
@en
prefLabel
Picosecond fluorescence decay of tryptophans in myoglobin
@ast
Picosecond fluorescence decay of tryptophans in myoglobin
@en
P2860
P356
P1476
Picosecond fluorescence decay of tryptophans in myoglobin
@en
P2093
R M Hochstrasser
P2860
P304
P356
10.1073/PNAS.81.14.4399
P407
P577
1984-07-01T00:00:00Z