Alteration of citrine structure by hydrostatic pressure explains the accompanying spectral shift

Barstow, Buz; Ando, Nozomi; Kim, Chae Un; Grüner, Sol M.

doi:10.1073/pnas.0802252105

Cited by 77 publications

(84 citation statements)

References 46 publications

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“…As shown in Figure 1 A, the l em of the sample gradually shifted from 539 nm at 0 MPa to approximately 534 nm at 360 MPa (a hypsochromic shift commensurate with that previously reported by Gruner [32] ). Frictional heating during compression appeared to contribute the overall response of the material through thermal denaturation of the protein (as evidenced by a reduction in fluorescence intensity; see the Supporting Information).…”

Section: Methodssupporting

confidence: 75%

Mechanically Modulating the Photophysical Properties of Fluorescent Protein Biocomposites for Ratio‐ and Intensiometric Sensors

et al. 2014

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Mechanically sensitive biocomposites comprised of fluorescent proteins report stress through distinct pathways. Whereas a composite containing an enhanced yellow fluorescent protein (eYFP) exhibited hypsochromic shifts in its fluorescence emission maxima following compression, a composite containing a modified green fluorescent protein (GFPuv) exhibited fluorescence quenching under the action of mechanical force. These ratio- and intensiometric sensors demonstrate that insights garnered from disparate fields (that is, polymer mechanochemistry and biophysics) can be harnessed to guide the rational design of new classes of biomechanophore-containing materials.

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Section: Methodssupporting

confidence: 75%

Mechanically Modulating the Photophysical Properties of Fluorescent Protein Biocomposites for Ratio‐ and Intensiometric Sensors

et al. 2014

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“…HDA ice was induced inside protein crystals by a high-pressure cryocooling method (23) originally developed for macromolecular crystallography (23)(24)(25)(26). The Bragg diffraction from protein crystals mainly provides information on protein structure.…”

mentioning

confidence: 99%

Evidence for liquid water during the high-density to low-density amorphous ice transition

Kim

Barstow²,

Täte

et al. 2009

Proc. Natl. Acad. Sci. U.S.A.

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Polymorphism of water has been extensively studied, but controversy still exists over the phase transition between high-density amorphous (HDA) and low-density amorphous (LDA) ice. We report the phase behavior of HDA ice inside high-pressure cryocooled protein crystals. Using X-ray diffraction, we demonstrate that the intermediate states in the temperature range from 80 to 170 K can be reconstructed as a linear combination of HDA and LDA ice, suggesting a first-order transition. We found evidence for a liquid state of water during the ice transition based on the protein crystallographic data. These observations open the possibility that the HDA ice induced by high-pressure cryocooling is a genuine glassy form of high-density liquid.liquid-liquid hypothesis ͉ supercooled water ͉ water phases ͉ high-density liquid S upercooled water shows anomalous thermodynamic behavior (1-3). Theories that account for these anomalous properties include the stability limit (4), the singularity-free (5, 6), and the liquid-liquid (LL) critical point (7) hypotheses. The latter 2 hypotheses propose the existence of 2 distinct forms of supercooled water: high-density liquid (HDL) and low-density liquid (LDL) water (8). In the singularity-free hypothesis, HDL transforms continuously to LDL. In the LL critical point theory, HDL undergoes a first-order phase transition to LDL (8). However, experimental study of the HDL-LDL phase transition is challenging as supercooled water spontaneously converts to crystalline forms below the homogeneous nucleation temperature (Ϸ235 K at 0.1 MPa). The transition between 2 glassy forms of water, high-density amorphous (HDA) and low-density amorphous (LDA) ice, has been extensively studied (9-18), as an analogue of the HDL-LDL transition. Controversy still exists as to whether the HDA-LDA ice transition is truly a first-order phase transition (10-13) or if it occurs because of a relaxation process of an unstable amorphous structure (15-18). More importantly, the connection between the HDA-LDA ice transition and the HDL-LDL phase transition, implied by thermodynamic and structural studies on water (19-22), remains challenging to prove experimentally (8).We used X-ray diffraction to study the transition of HDA to LDA ice in protein crystals. HDA ice was induced inside protein crystals by a high-pressure cryocooling method (23) originally developed for macromolecular crystallography (23-26). The Bragg diffraction from protein crystals mainly provides information on protein structure. The simultaneously recorded water diffuse diffraction (WDD) profile reports on the phase of the water in the protein crystal, which accounts for typically 40-60% of its volume. Fig. 1 shows diffraction images and the WDD profiles from a high-pressure cryocooled crystal of the globular protein thaumatin. As the crystal temperature is increased from 80 to 170 K, the primary WDD peak, corresponding to the mean distance between neighboring water molecule oxygen atoms, shifts to lower momentum transfer (Q) region [Q ϭ 4 sin( )/ , wh...

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“…Cryocooling was used by Barstow and coworkers [76] on crystals of Yellow Fluorescent Protein (YFP) Aequorea citrine, an intrinsically fluorescent and extremely bright protein. In total, 26 structures at pressures 50 to 500 MPa were quenched at a low temperature and refined with resolution limits ranging from 1.5 Å to 2.46 Å.…”

Section: High Pressure Crycoolingmentioning

confidence: 99%

High pressure macromolecular crystallography for structural biology: a review

Kurpiewska

Lewiński

2010

Open Life Sciences

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Abstract:In recent years, significant progress in high pressure macromolecular crystallography has been observed. It can be attributed both to the developments in experimental techniques, as well as to recognition of importance of high pressure protein studies in biochemistry and biophysics. The number of protein structures determined at pressure up to 1 GPa is growing. The unique advantages of this method can greatly improve the investigation of higher energy conformers of functional significance and our understandingoffunctionallyimportantconformers,proteinfoldingprocessesandthestructuralbaseofconformationaldiseases.

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Alteration of citrine structure by hydrostatic pressure explains the accompanying spectral shift

Cited by 77 publications

References 46 publications

Mechanically Modulating the Photophysical Properties of Fluorescent Protein Biocomposites for Ratio‐ and Intensiometric Sensors

Mechanically Modulating the Photophysical Properties of Fluorescent Protein Biocomposites for Ratio‐ and Intensiometric Sensors

Evidence for liquid water during the high-density to low-density amorphous ice transition

High pressure macromolecular crystallography for structural biology: a review

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