Time-resolved fluorescence and proton NMR studies of tyrosyl residues in oxytocin and small peptides: correlation of NMR-determined conformations of tyrosyl residues and fluorescence decay kinetics

Biochemistry ◽  
1986 ◽  
Vol 25 (3) ◽  
pp. 607-612 ◽  
Author(s):  
J. B. Alexander Ross ◽  
William R. Laws ◽  
Angeliki Buku ◽  
John Clark Sutherland ◽  
Herman R. Wyssbrod
Keyword(s):  
Proton Nmr ◽  
Fluorescence Decay ◽  
Time Resolved Fluorescence ◽  
Decay Kinetics ◽  
Small Peptides ◽  
Nmr Studies ◽  
Time Resolved ◽  
Fluorescence Decay Kinetics

Monitoring Supramolecular Self-Assembly using Time-Resolved Fluorescence Spectroscopy

2011 ◽  
Vol 64 (6) ◽  
pp. 825 ◽  
Author(s):  
Scott C. McLean ◽  
Colin A. Scholes ◽  
Trevor A. Smith ◽  
Michelle L. Gee
Keyword(s):  
Fluorescence Spectroscopy ◽  
Self Assembly ◽  
Supramolecular Structure ◽  
Micelle Formation ◽  
Fluorescence Decay ◽  
Distribution Analysis ◽  
Time Resolved Fluorescence ◽  
Decay Kinetics ◽  
Time Resolved ◽  
Relative Population

Time-resolved fluorescence spectroscopy is used to observe subtleties in supramolecular structure during the self-assembly of polymers in solution. Lifetime distribution analysis of the fluorescence decay kinetics of the solvent-sensitive fluorescent probe 1-anilino-8-naphthalene sulfonic acid associated with the di-block copolymer poly(2-vinylpyridine)41–poly(ethylene oxide)204 (P2VP-PEO) as it self-assembles enabled identification of three microdomains, distinguishable on the basis of micropolarity. These microdomains can be assigned to different supramolecular substructures: the micelle corona (high polarity), the micelle core and the P2VP globule (both low polarity), and the core–corona interface and the globule–PEO junction (both intermediate polarity). Changes in the relative population distributions of these sub-structures as a function of P2VP-PEO pinpoint the onset of micellization corresponding to the critical micelle concentration (CMC) of the copolymer, but indicate significant variation in supramolecular structure, including micelle formation, well below the CMC. This suggests that supramolecular self-assembly in polymeric systems has characteristics of a second order phase transition.

Time-resolved fluorescence and proton NMR studies of tyrosine and tyrosine analogs: correlation of NMR-determined rotamer populations and fluorescence kinetics

Biochemistry ◽  
1986 ◽  
Vol 25 (3) ◽  
pp. 599-607 ◽  
Author(s):  
William R. Laws ◽  
J. B. Alexander Ross ◽  
Herman R. Wyssbrod ◽  
Joseph M. Beechem ◽  
Ludwig Brand ◽  
...  
Keyword(s):  
Proton Nmr ◽  
Time Resolved Fluorescence ◽  
Nmr Studies ◽  
Time Resolved ◽  
Fluorescence Kinetics

scholarly journals Architecture of Polyglutamine-containing Fibrils from Time-resolved Fluorescence Decay

2014 ◽  
Vol 289 (39) ◽  
pp. 26817-26828 ◽  
Author(s):  
Christoph Röthlein ◽  
Markus S. Miettinen ◽  
Tejas Borwankar ◽  
Jörg Bürger ◽  
Thorsten Mielke ◽  
...  
Keyword(s):  
Fluorescence Decay ◽  
Time Resolved Fluorescence ◽  
Time Resolved

The tryptophan fluorescence lifetime puzzle. A study of decay times in aqueous solution as a function of pH and buffer composition

1981 ◽  
Vol 59 (7) ◽  
pp. 1037-1044 ◽  
Author(s):  
Eva Gudgin ◽  
Ricardo Lopez-Delgado ◽  
William R. Ware
Keyword(s):  
Tryptophan Fluorescence ◽  
Fluorescence Decay ◽  
Low Ph ◽  
Decay Kinetics ◽  
Decay Component ◽  
Diffusion Controlled ◽  
Double Exponential ◽  
Decay Times ◽  
Fluorescence Decay Kinetics ◽  
Buffer Composition

Tryptophan fluorescence decay kinetics have been systematically investigated in aqueous solutions as a function of pH as well as in a variety of buffer solutions. Below pH 7.0, the decay appears to be double exponential with a subnanosecond component confirming the previous findings of Rayner and Szabo (3). In the low pH region, where the proton concentration becomes kinetically significant, tryptophan fluorescence is collisionally quenched by [H+] with diffusion controlled rate and no experimental evidence is found regarding the appearance at low pH of a new tryptophan molecular species, namely the cationic form. At pH ≥ 7.0, the decay becomes triple-exponential with the appearance of a long component whose contribution to the total emission intensity increases rapidly with increasing pH at the expense of the other two. Lifetimes and relative intensities of each decay component depend in a complex way on pH and on the buffer chemical composition.

scholarly journals Evidence that D1 Processing Is Required for Manganese Binding and Extrinsic Protein Assembly into Photosystem II

2004 ◽  
Vol 279 (44) ◽  
pp. 45417-45422 ◽  
Author(s):  
Johnna L. Roose ◽  
Himadri B. Pakrasi
Keyword(s):  
Photosystem Ii ◽  
Mutant Cell ◽  
Protein A ◽  
D1 Protein ◽  
Fluorescence Decay ◽  
Normal Function ◽  
Temporal Position ◽  
Decay Kinetics ◽  
Fluorescence Decay Kinetics ◽  
Extrinsic Proteins

Photosystem II (PSII) is a large membrane protein complex that catalyzes oxidation of water to molecular oxygen. During its normal function, PSII is damaged and frequently turned over. The maturation of the D1 protein, a key component in PSII, is a critical step in PSII biogenesis. The precursor form of D1 (pD1) contains a C-terminal extension, which is removed by the protease CtpA to yield PSII complexes with oxygen evolution activity. To determine the temporal position of D1 processing in the PSII assembly pathway, PSII complexes containing only pD1 were isolated from a CtpA-deficient strain of the cyanobacteriumSynechocystis6803. Although membranes from the mutant cell had nearly 50% manganese, no manganese was detected in isolated ΔctpAHT3 PSII, indicating a severely decreased manganese affinity. However, chlorophyll fluorescence decay kinetics after a single saturating flash suggested that the donor YZwas accessible to exogenous Mn2+ions. Furthermore, the extrinsic proteins PsbO, PsbU, and PsbV were not present in PSII isolated from this mutant. However, PsbO and PsbV were present in mutant membranes, but the amount of PsbV protein was consistently less in the mutant membranes compared with the control membranes. We conclude that D1 processing precedes manganese binding and assembly of the extrinsic proteins into PSII. Interestingly, the Psb27 protein was found to be more abundant in ΔctpAHT3 PSII than in HT3 PSII, suggesting a possible role of Psb27 as an assembly factor during PSII biogenesis.

scholarly journals Analysis of Fluorescence Decay Kinetics of Indocyanine Green Monomers and Aggregates in Brain Tumor Model In Vivo

Nanomaterials ◽  
2021 ◽  
Vol 11 (12) ◽  
pp. 3185
Author(s):  
Dina Farrakhova ◽  
Igor Romanishkin ◽  
Yuliya Maklygina ◽  
Lina Bezdetnaya ◽  
Victor Loschenov
Keyword(s):  
Brain Tumor ◽  
Indocyanine Green ◽  
Fluorescence Lifetime ◽  
Tumor Model ◽  
Fluorescence Decay ◽  
Decay Kinetics ◽  
Lifetime Analysis ◽  
Fluorescence Decay Kinetics ◽  
Brain Tumor Model

Spectroscopic approach with fluorescence time resolution allows one to determine the state of a brain tumor and its microenvironment via changes in the fluorescent dye’s fluorescence lifetime. Indocyanine green (ICG) is an acknowledged infra-red fluorescent dye that self-assembles into stable aggregate forms (ICG NPs). ICG NPs aggregates have a tendency to accumulate in the tumor with a maximum accumulation at 24 h after systemic administration, enabling extended intraoperative diagnostic. Fluorescence lifetime analysis of ICG and ICG NPs demonstrates different values for ICG monomers and H-aggregates, indicating promising suitability for fluorescent diagnostics of brain tumors due to their affinity to tumor cells and stability in biological tissue.

Maximum likelihood method for the analysis of time-resolved fluorescence decay curves

1991 ◽  
Vol 20 (5) ◽  
pp. 247-262 ◽  
Author(s):  
?eljko Bajzer ◽  
Terry M. Therneau ◽  
Joseph C. Sharp ◽  
Franklin G. Prendergast
Keyword(s):  
Maximum Likelihood ◽  
Maximum Likelihood Method ◽  
Fluorescence Decay ◽  
Likelihood Method ◽  
Time Resolved Fluorescence ◽  
Time Resolved
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