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Alphas and taus of tryptophan fluorescence in membranes

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Alphas and taus of tryptophan fluorescence in membranes (English)

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A S Ladokhin

1

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S H White

series ordinal

2

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language of work or name

English

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publication date

September 2001

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published in

Biophysical Journal

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volume

81

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issue

3

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page(s)

1825-7

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cites work

Ionization, partitioning, and dynamics of tryptophan octyl ester: implications for membrane-bound tryptophan residues

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The structure and orientation of class-A amphipathic peptides on a phospholipid bilayer surface

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Tryptophan rotamer distributions in amphipathic peptides at a lipid surface

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Site-specific tryptophan dynamics in class A amphipathic helical peptides at a phospholipid bilayer interface

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Tryptophan octyl ester in detergent micelles of dodecylmaltoside: fluorescence properties and quenching by brominated detergent analogs

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Nanosecond dynamics of charged fluorescent probes at the polar interface of a membrane phospholipid bilayer.

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Fluorescence measurements of environmental relaxation at the lipid-water interface region of bilayer membranes

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Selective laser spectroscopy of 1-phenylnaphthylamine in phospholipid membranes.

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Lifetime distributions and anisotropy decays of indole fluorescence in cyclohexane/ethanol mixtures by frequency-domain fluorometry.

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An amphipathic alpha-helix at a membrane interface: a structural study using a novel X-ray diffraction method.

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Multiple-domain fluorescence lifetime data analysis

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Fluorescence of membrane-bound tryptophan octyl ester: a model for studying intrinsic fluorescence of protein-membrane interactions

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On spectral relaxation in proteins.

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Time-resolved fluorescence and 1H NMR studies of tyrosine and tyrosine analogues: correlation of NMR-determined rotamer populations and fluorescence kinetics

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Analysis of time-resolved fluorescence anisotropy in lipid-protein systems. II. Application to tryptophan fluorescence of bacteriophage M13 coat protein incorporated in phospholipid bilayers

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Orientational distribution of 1,6-diphenyl-1,3,5-hexatriene in phospholipid vesicles as determined by global analysis of frequency domain fluorimetry data.

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Hydrophobic interactions of peptides with membrane interfaces.

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Structure of a fluid dioleoylphosphatidylcholine bilayer determined by joint refinement of x-ray and neutron diffraction data. III. Complete structure

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Identifiers

DOI

10.1016/S0006-3495(01)75833-X

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PMC publication ID

1301657

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PubMed publication ID

11525196

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(Q28346910)

Alphas and taus of tryptophan fluorescence in membranes

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