Exploring Chromophore−Protein Interactions in Fluorescent Protein cmFP512 fromCerianthus membranaceus:  X-ray Structure Analysis and Optical Spectroscopy†

Biochemistry ◽  
2006 ◽  
Vol 45 (43) ◽  
pp. 12942-12953 ◽  
Author(s):  
Karin Nienhaus ◽  
Fabiana Renzi ◽  
Beatrice Vallone ◽  
Jörg Wiedenmann ◽  
G. Ulrich Nienhaus
Keyword(s):  
Optical Spectroscopy ◽  
Structure Analysis ◽  
Protein Interactions ◽  
Fluorescent Protein ◽  
X Ray

scholarly journals Dynamic tuning of FRET in a green fluorescent protein biosensor

2019 ◽  
Vol 5 (8) ◽  
pp. eaaw4988 ◽  
Author(s):  
Pablo Trigo-Mourino ◽  
Thomas Thestrup ◽  
Oliver Griesbeck ◽  
Christian Griesinger ◽  
Stefan Becker
Keyword(s):  
Green Fluorescent Protein ◽  
Protein Interactions ◽  
Fluorescent Protein ◽  
Fluorescent Proteins ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Structural Data ◽  
X Ray ◽  
Dynamic Tuning ◽  
Green Fluorescent

Förster resonance energy transfer (FRET) between mutants of green fluorescent protein is widely used to monitor protein-protein interactions and as a readout mode in fluorescent biosensors. Despite the fundamental importance of distance and molecular angles of fluorophores to each other, structural details on fluorescent protein FRET have been missing. Here, we report the high-resolution x-ray structure of the fluorescent proteins mCerulean3 and cpVenus within the biosensor Twitch-2B, as they undergo FRET and characterize the dynamics of this biosensor with B02-dependent paramagnetic nuclear magnetic resonance at 900 MHz and 1.1 GHz. These structural data provide the unprecedented opportunity to calculate FRET from the x-ray structure and to compare it to experimental data in solution. We find that interdomain dynamics limits the FRET effect and show that a rigidification of the sensor further enhances FRET.

scholarly journals Improved Photocleavable Proteins with Faster and More Efficient Dissociation

2020 ◽  
Author(s):  
Xiaocen Lu ◽  
Yurong Wen ◽  
Shuce Zhang ◽  
Wei Zhang ◽  
Yilun Chen ◽  
...  
Keyword(s):  
Protein Interactions ◽  
First Generation ◽  
Fluorescent Protein ◽  
Cultured Cells ◽  
Protein Localization ◽  
Contrast Ratio ◽  
Cell Physiology ◽  
Protein Protein Interactions ◽  
X Ray ◽  
Chain Cleavage

AbstractThe photocleavable protein (PhoCl) is a green-to-red photoconvertible fluorescent protein that, when illuminated with violet light, undergoes main chain cleavage followed by spontaneous dissociation of the resulting fragments. The first generation PhoCl (PhoCl1) exhibited a relative slow rate of dissociation, potentially limiting its utilities for optogenetic control of cell physiology. In this work, we report the X-ray crystal structures of the PhoCl1 green state, red state, and cleaved empty barrel. Using structure-guided engineering and directed evolution, we have developed PhoCl2c with higher contrast ratio and PhoCl2f with faster dissociation. We characterized the performance of these new variants as purified proteins and expressed in cultured cells. Our results demonstrate that PhoCl2 variants exhibit faster and more efficient dissociation, which should enable improved optogenetic manipulations of protein localization and protein-protein interactions in living cells.

Absolute Stereochemistry of (-)-Wieland-Miescher Ketone as Established by the X-ray Crystallographic and CD Exciton Chirality Methods

1992 ◽  
Vol 57 (7) ◽  
pp. 1459-1465 ◽  
Author(s):  
Nobuyuki Harada ◽  
Tatsuo Sugioka ◽  
Hisashi Uda ◽  
Takeo Kuriki
Keyword(s):  
Structure Analysis ◽  
Absolute Configuration ◽  
X Ray ◽  
The Absolute ◽  
Absolute Stereochemistry

The 8aR absolute stereochemistry of Wieland-Miescher ketone (-)-I was established by the X-ray structure analysis of its bis(4-bromobenzoate) derivatives (1R,6R,8aR)-(+)-IV and (1R,6S,8aR)-(-)-V. The absolute configuration of (-)-I was corroborated further by the application of the CD exciton chirality method to bis(4-bromobenzoates) (+)-IV and (-)-V.

scholarly journals Preparative-scale HPLC Resolution of Metallacyclic η3-Allyltricarbonyliron Complexes and Determination of the Absolute Configuration by X-Ray Crystal Structure Analysis

1999 ◽  
Vol 23 (9) ◽  
pp. 578-579
Author(s):  
Rainer Schobert ◽  
Hermann Pfab ◽  
Jutta Böhmer ◽  
Frank Hampel ◽  
Andreas Werner
Keyword(s):  
Crystal Structure ◽  
Silica Gel ◽  
Structure Analysis ◽  
Absolute Configuration ◽  
Crystal Structure Analysis ◽  
Preparative Scale ◽  
X Ray ◽  
The Absolute

Racemates of (η3-allyl)tricarbonyliron lactone complex Fe(CO)3{η1:η3-C(O)XCH2CHCMeCH2} 1a (X = O) and (η3-allyl)tricarbonyliron lactam complex 2a (X = NMe) are resolved on a preparative scale by HPLC on cellulose tris(3,5-dimethylphenyl)carbamate/silica gel RP-8 and the absolute configuration of (-)-2a is determined by X-ray crystal structure analysis.

scholarly journals NMR, X-Ray and MS Investigations of Ethyl 2-Aroyl-and Ethyl 2-Arylcarbamoyl-4,5- dimethyl-1,2,3,6-tetrahydropyridazine-1- carboxylates: Flexible Multidentate Ligands

1999 ◽  
Vol 23 (3) ◽  
pp. 186-187
Author(s):  
Erkki Kolehmainen ◽  
Katri Laihia ◽  
Maija Nissinen ◽  
Kalevi Pihlaja ◽  
Alexander Perjéssy ◽  
...  
Keyword(s):  
Structure Analysis ◽  
Multidentate Ligands ◽  
X Ray ◽  
C Nmr

The 1H and 13C NMR spectral assignments of ethyl 2-aroyl-4,5-dimethyl-1,2,3,6-tetrahydropyridazine-1-carboxylates (1a-1h) and ethyl 2-arylcarbamoyl-4,5-dimethyl-1,2,3,6-tetrahydropyridazine-1-carboxylates (2a-2k) are given based on DQF COSY, 1H,13C HMQC and 1H,13C HMBC-measurements; the dynamics of the tetrahydropyridazine ring has been studied by 1H, 1H EXSY-technique and the structure of one congener (4′-methylphenyl-derivative, 2a) has been confirmed by X-ray structure analysis.

Second-Generation Inhibitors for the Metalloprotease Neprilysin Based on Bicyclic Heteroaromatic Scaffolds: Synthesis, Biological Activity, and X-Ray Crystal-Structure Analysis

2005 ◽  
Vol 88 (4) ◽  
pp. 731-750 ◽  
Author(s):  
Stefan Sahli ◽  
Brian Frank ◽  
W. Bernd Schweizer ◽  
François Diederich ◽  
Denise Blum-Kaelin ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Biological Activity ◽  
Structure Analysis ◽  
Second Generation ◽  
Crystal Structure Analysis ◽  
X Ray

Regiospezifische Insertion von [SCN]- und [SeCN]- in die S – C- bzw. Se– C-Bindung Übergangsmetall-koordinierter Thietane und SelenetaneRegiospecific Insertion of [SCN]- and [SeCN]- in the S–C- and Se–C-Bond of Transition-Metal-Coordinated Thietanes and Selenetanes

1993 ◽  
Vol 48 (11) ◽  
pp. 1613-1620 ◽  
Author(s):  
Helmut Fischer ◽  
Claudia Kalbas ◽  
Carsten Troll ◽  
Klaus H. Fluck
Keyword(s):  
Nitrogen Atom ◽  
Transition Metal ◽  
Structure Analysis ◽  
Trans Isomer ◽  
X Ray ◽  
Tungsten Complexes ◽  
Membered Heterocycle

Pentacarbonyl(thietane)tungsten complexes react with thiocyanate, [SCN]-, and SiO2/H2O by insertion of the CN group into a S—C bond of the four-membered heterocycle, 1,3-migration of the pentacarbonyltungsten fragment and protonation of the nitrogen atom to give tungsten-coordinated thiazinthione complexes. Analogously, the reactions of a thietane tungsten complex with [SeCN]- and SiO2/H2O affords a thiazinselone complex. A selenazinthione complex is obtained from a selenetane complex and [SCN]- (+ SiO2/H2O). The insertions are regiospecific and stereoselective. The structure of the trans-isomer of a pentacarbonyl-(thiazinthione) complex has been established by X-ray structure analysis.

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