Dynamics of the hydrate and amide groups of crystalline ribonuclease and lysozyme

Usha, M.G.; Speyer, Julia B.; Wittebort, Richard J.

doi:10.1016/0301-0104(91)87084-9

Cited by 14 publications

(18 citation statements)

References 26 publications

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“…The narrow peak originates from the mobile core and NCR water that we have characterized by MRD measurements. The shape and width of the broad component is consistent with exchangeable ND and OD deuterons (with a distribution of orientational order parameters) in immobilized macromolecules, [39][40][41] henceforth referred to as labile deuterons (LDs). But the broad component is also consistent with immobilized D 2 O molecules or with a combination of LDs and immobilized water.…”

Section: Water Mobility In the Corementioning

confidence: 62%

“…2.2), the broad component is not fully excited and its intensity is therefore reduced by a factor of 0.76. 39,40 Taking this factor into account, we find that the broad component corresponds to 6.7 ± 0.3 % of the deuterons in the sample. The water content of the Mn-depleted sample used for the quadrupolar echo experiment was h = 1.25 g D 2 O (g dry spore mass) −1 .…”

Section: Water Mobility In the Corementioning

confidence: 94%

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Mobility of Core Water in Bacillus subtilis Spores by 2H NMR

Kaieda

Setlow

et al. 2013

Biophysical Journal

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Bacterial spores in a metabolically dormant state can survive long periods without nutrients under extreme environmental conditions. The molecular basis of spore dormancy is not well understood, but the distribution and physical state of water within the spore is thought to play an important role. Two scenarios have been proposed for the spore's core region, containing the DNA and most enzymes. In the gel scenario, the core is a structured macromolecular framework permeated by mobile water. In the glass scenario, the entire core, including the water, is an amorphous solid and the quenched molecular diffusion accounts for the spore's dormancy and thermal stability. Here, we use (2)H magnetic relaxation dispersion to selectively monitor water mobility in the core of Bacillus subtilis spores in the presence and absence of core Mn(2+) ions. We also report and analyze the solid-state (2)H NMR spectrum from these spores. Our NMR data clearly support the gel scenario with highly mobile core water (~25 ps average rotational correlation time). Furthermore, we find that the large depot of manganese in the core is nearly anhydrous, with merely 1.7% on average of the maximum sixfold water coordination.

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Section: Water Mobility In the Corementioning

confidence: 62%

Section: Water Mobility In the Corementioning

confidence: 94%

Mobility of Core Water in Bacillus subtilis Spores by 2H NMR

Kaieda

Setlow

et al. 2013

Biophysical Journal

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“…The absences of a glass transition and of ice formation in the solvent channels of HEWL crystals may be explained by the very small size of these channels (14 A ˚in diameter), resulting from the tight packing of the macromolecules in the lattice. A substantial fraction of water molecules are ordered in the crystal channels (.70% of them is required for monolayer coverage of the protein molecules (Usha et al, 1991)) and an extended three-dimensional hydrate lattice may not form. Viscous drag forces are generated, hindering unordered water molecules from freely reorienting as the temperature is elevated.…”

Section: Solvent Behavior In Crystals Ofmentioning

confidence: 99%

Temperature Derivative Fluorescence Spectroscopy as a Tool to Study Dynamical Changes in Protein Crystals

Weik

Vernède

Royant

et al. 2004

Biophysical Journal

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Motions through the energy landscape of proteins lead to biological function. At temperatures below a dynamical transition (150-250 K), some of these motions are arrested and the activity of some proteins ceases. Here, we introduce the technique of temperature-derivative fluorescence microspectrophotometry to investigate the dynamical behavior of single protein crystals. The observation of glass transitions in thin films of water/glycerol mixtures allowed us to demonstrate the potential of the technique. Then, protein crystals were investigated, after soaking the samples in a small amount of fluorescein. If the fluorophore resides within the crystal channels, temperature-dependent changes in solvent dynamics can be monitored. Alternatively, if the fluorophore binds to the protein, local dynamical transitions within the biomolecule can be probed directly. A clear dynamical transition was observed at 175 K in the active site of crystalline human butyrylcholinesterase. The results suggest that the dynamics of crystalline proteins is strongly dependent on solvent composition and confinement in the crystal channels. Beyond applications in the field of kinetic crystallography, the highly sensitive temperature-derivative fluorescence microspectrophotometry technique opens the way to many studies on the dynamics of biological nanosamples.

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“…Solid state NMR experiments show that water deuterium atoms in crystals of lysozyme (26), ribonuclease (26), and crambin (27) undergo a mobile to stationary transition at Ϸ180 K. Water dynamics in crambin crystals match these enzymes. Further, the hydrophobic͞hydrophilic accessible surface area in crambin crystals is very close to that found in carboxypeptidase and myoglobin crystals (28).…”

mentioning

confidence: 99%