On the nature of a glassy state of matter in a hydrated protein: Relation to protein function

Teeter, Martha M.; Yamano, Akihito; Stec, Boguslaw; Mohanty, Udayan

doi:10.1073/pnas.201404398

Cited by 122 publications

(113 citation statements)

References 54 publications

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“…265) water molecules in the hydration layer. This result is hardly compatible with the existence of extensive hydrogen-bond networks of fused water polygons, as inferred from cryocrystallographic studies of several proteins (Nakasako 1999;Esposito et al 2000;Teeter et al 2001). As discussed in § 4, these networks are likely to be cryo-artefacts, formed when water motions are quenched at ca.…”

Section: Magnetic Relaxation As a Probe Of Protein Hydration Dynamicsmentioning

confidence: 77%

“…However, 2 H and 17 O MRD studies indicate a mere twofold dynamic retardation for the vast majority of water molecules in the hydration layer of proteins (see § 5a). For the small protein crambin, where ultrahigh-resolution structures have been reported at several temperatures from 100 K to 293 K, the 6-and 7-membered rings disappear above 200 K (Teeter et al 2001), suggesting that they are, in fact, cryo-artefacts.…”

Section: Structure Of Protein Hydrationmentioning

confidence: 99%

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Protein hydration dynamics in solution: a critical survey

Halle

2004

Phil. Trans. R. Soc. Lond. B

499

576

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The properties of water in biological systems have been studied for well over a century by a wide range of physical techniques, but progress has been slow and erratic. Protein hydration-the perturbation of water structure and dynamics by the protein surface-has been a particularly rich source of controversy and confusion. Our aim here is to critically examine central concepts in the description of protein hydration, and to assess the experimental basis for the current view of protein hydration, with the focus on dynamic aspects. Recent oxygen-17 magnetic relaxation dispersion (MRD) experiments have shown that the vast majority of water molecules in the protein hydration layer suffer a mere twofold dynamic retardation compared with bulk water. The high mobility of hydration water ensures that all thermally activated processes at the protein-water interface, such as binding, recognition and catalysis, can proceed at high rates. The MRD-derived picture of a highly mobile hydration layer is consistent with recent molecular dynamics simulations, but is incompatible with results deduced from intermolecular nuclear Overhauser effect spectroscopy, dielectric relaxation and fluorescence spectroscopy. It is also inconsistent with the common view of hydration effects on protein hydrodynamics. Here, we show how these discrepancies can be resolved.

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Section: Magnetic Relaxation As a Probe Of Protein Hydration Dynamicsmentioning

confidence: 77%

Section: Structure Of Protein Hydrationmentioning

confidence: 99%

Protein hydration dynamics in solution: a critical survey

Halle

2004

Phil. Trans. R. Soc. Lond. B

499

576

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“…The dMSD/dT values obtained from crystals of myoglobin (Parak et al, 1982;Chong et al, 2001), ribonuclease A (Tilton et al, 1992;Rasmussen et al, 1992), lysozyme (Joti et al, 2002), maltose binding protein (Wood et al, 2008) and purple membrane (Wood et al, 2007) are in the range 10 À4 -10 À3 Å 2 K À1 ; the rate for hexagonal ice is $2 Â 10 À4 Å 2 K À1 (Teeter et al, 2001). These studies followed a variety of thermal trajectories from room temperature to the measurement temperature, including slow cooling and warming to each temperature (Parak et al, 1982;Wood et al, 2007Wood et al, , 2008, quenching from room temperature to each measurement temperature (Tilton et al, 1992;Rasmussen et al, 1992;Chong et al, 2001;Teeter et al, 2001), and quenching to low temperature and then slowly warming to each measurement temperature (Joti et al, 2002). If the entire change in B is due to changes in harmonic motions, then thaumatin must be an unusually 'stiff' protein in this temperature range.…”

Section: Comparison With Previous Workmentioning

confidence: 99%

“…For example, Tilton et al reported that at T = 200 K a ribonuclease A crystal rapidly became opaque and ceased to diffract, despite the use of 50%(v/v) 2-methyl-2,4-pentanediol (MPD). The only successes at this temperature used a methanol concentration of 75%(v/v) (Singh et al, 1980), or crambin, an unusually small and dry protein crystal system (Teeter et al, 2001).…”

Section: Introductionmentioning

confidence: 99%

Slow cooling of protein crystals

Warkentin¹,

Thorne²

2009

J Appl Crystallogr

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Cryoprotectant-free thaumatin crystals have been cooled from 300 to 100 K at a rate of 0.1 K s À1 -10 3 -10 4 times slower than in conventional flash coolingwhile continuously collecting X-ray diffraction data, so as to follow the evolution of protein lattice and solvent properties during cooling. Diffraction patterns show no evidence of crystalline ice at any temperature. This indicates that the lattice of protein molecules is itself an excellent cryoprotectant, and with sodium potassium tartrate incorporated from the 1.5 M mother liquor ice nucleation rates are at least as low as in a 70% glycerol solution. Crystal quality during slow cooling remains high, with an average mosaicity at 100 K of 0.2 . Most of the mosaicity increase occurs above $200 K, where the solvent is still liquid, and is concurrent with an anisotropic contraction of the unit cell. Near 180 K a crossover to solid-like solvent behavior occurs, and on further cooling there is no additional degradation of crystal order. The variation of B factor with temperature shows clear evidence of a protein dynamical transition near 210 K, and at lower temperatures the slope dB/dT is a factor of 3-6 smaller than has been reported for any other protein. These results establish the feasibility of fully temperature controlled studies of protein structure and dynamics between 300 and 100 K.

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“…In the last several years it has become rather obvious that proteins have a special nature that appears to be a non-ergodic glassy state that combines the features of two different states of matter: the solid and the liquid states (Fenimore et al, 2004;Teeter et al, 2001). This dual nature of proteins is reflected in protein crystal structures by two contrasting features.…”

mentioning

confidence: 99%

Comment onStereochemical restraints revisited: how accurate are refinement targets and how much should protein structures be allowed to deviate from them?by Jaskolski, Gilski, Dauter & Wlodawer (2007)

Stec

2007

Acta Crystallogr D Biol Cryst

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On the nature of a glassy state of matter in a hydrated protein: Relation to protein function

Cited by 122 publications

References 54 publications

Protein hydration dynamics in solution: a critical survey

Protein hydration dynamics in solution: a critical survey

Slow cooling of protein crystals

Comment onStereochemical restraints revisited: how accurate are refinement targets and how much should protein structures be allowed to deviate from them?by Jaskolski, Gilski, Dauter & Wlodawer (2007)

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