Quantitative measurement of optical parameters in normal breasts using time-resolved spectroscopy: in vivo results of 30 Japanese women

1996 ◽  
Vol 1 (3) ◽  
pp. 330 ◽  
Author(s):  
Kazunori Suzuki
Keyword(s):  
Quantitative Measurement ◽  
Japanese Women ◽  
Optical Parameters ◽  
Time Resolved ◽  
Time Resolved Spectroscopy

In vivo time-resolved spectroscopy of the human bronchial early cancer autofluorescence

2009 ◽  
Vol 14 (2) ◽  
pp. 024011 ◽  
Author(s):  
Pascal Uehlinger ◽  
Tanja Gabrecht ◽  
Thomas Glanzmann ◽  
Jean-Pierre Ballini ◽  
Alexandre Radu ◽  
...  
Keyword(s):  
Early Cancer ◽  
Time Resolved ◽  
Time Resolved Spectroscopy

scholarly journals In vivo optical characterization of human prostate tissue using near-infrared time-resolved spectroscopy

2007 ◽  
Vol 12 (1) ◽  
pp. 014022 ◽  
Author(s):  
Tomas Svensson ◽  
Stefan Andersson-Engels ◽  
Margrét Einarsdóttír ◽  
Katarina Svanberg
Keyword(s):  
Near Infrared ◽  
Optical Characterization ◽  
Prostate Tissue ◽  
Human Prostate ◽  
Time Resolved ◽  
Time Resolved Spectroscopy ◽  
Human Prostate Tissue

scholarly journals Real-time observation of tetrapyrrole binding to an engineered bacterial phytochrome

2021 ◽  
Vol 4 (1) ◽  
Author(s):  
Yusaku Hontani ◽  
Mikhail Baloban ◽  
Francisco Velazquez Escobar ◽  
Swetta A. Jansen ◽  
Daria M. Shcherbakova ◽  
...  
Keyword(s):  
Real Time ◽  
Rational Design ◽  
Near Infrared ◽  
Fluorescent Proteins ◽  
Covalent Bond ◽  
Binding Pocket ◽  
Tissue Imaging ◽  
Covalent Attachment ◽  
Time Resolved

AbstractNear-infrared fluorescent proteins (NIR FPs) engineered from bacterial phytochromes are widely used for structural and functional deep-tissue imaging in vivo. To fluoresce, NIR FPs covalently bind a chromophore, such as biliverdin IXa tetrapyrrole. The efficiency of biliverdin binding directly affects the fluorescence properties, rendering understanding of its molecular mechanism of major importance. miRFP proteins constitute a family of bright monomeric NIR FPs that comprise a Per-ARNT-Sim (PAS) and cGMP-specific phosphodiesterases - Adenylyl cyclases - FhlA (GAF) domain. Here, we structurally analyze biliverdin binding to miRFPs in real time using time-resolved stimulated Raman spectroscopy and quantum mechanics/molecular mechanics (QM/MM) calculations. Biliverdin undergoes isomerization, localization to its binding pocket, and pyrrolenine nitrogen protonation in <1 min, followed by hydrogen bond rearrangement in ~2 min. The covalent attachment to a cysteine in the GAF domain was detected in 4.3 min and 19 min in miRFP670 and its C20A mutant, respectively. In miRFP670, a second C–S covalent bond formation to a cysteine in the PAS domain occurred in 14 min, providing a rigid tetrapyrrole structure with high brightness. Our findings provide insights for the rational design of NIR FPs and a novel method to assess cofactor binding to light-sensitive proteins.

scholarly journals Photophysical properties and fluorosolvatochromism of D–π–A thiophene based derivatives

RSC Advances ◽  
2020 ◽  
Vol 10 (71) ◽  
pp. 43459-43471
Author(s):  
Hussain A. Z. Sabek ◽  
Ahmed M. M. Alazaly ◽  
Dina Salah ◽  
Hesham S. Abdel-Samad ◽  
Mohamed A. Ismail ◽  
...  
Keyword(s):  
Photophysical Properties ◽  
Fluorescence Emission ◽  
Time Resolved ◽  
Time Resolved Spectroscopy ◽  
Solvation Models

Solvation-dependent photophysical properties of two push–pull thiophene-based compounds with donor–π–acceptor (D–π–A) structures were investigated using absorption, fluorescence emission and time resolved spectroscopy, and supported by different solvation models.

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