Cold denaturation of myoglobin

Privalov, Peter L.; Griko, Yu.V.; Venyaminov, Sergei Yu.; Kutyshenko, V. P.

doi:10.1016/0022-2836(86)90017-3

Cited by 438 publications

(371 citation statements)

References 37 publications

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“…Although the exact underlying mechanism of this phenomenon is still unclear, some studies have proposed a role of non-polar groups in unfolding of proteins due to cold denaturation (Dias et al, 2010;Privalov, 1990). From a thermodynamic perspective, the hydration of non-polar groups in a protein is favorable as this releases Gibb's energy of hydration, which is negative, and increases in magnitude at lower temperatures.…”

Section: V223 Sensitivity Of Fluc Variants To Cold Denaturationmentioning

confidence: 99%

Firefly luciferase mutants as sensors of proteome stress

et al. 2011

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Section: V223 Sensitivity Of Fluc Variants To Cold Denaturationmentioning

confidence: 99%

Firefly luciferase mutants as sensors of proteome stress

et al. 2011

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“…But high temperature stress (although the classical activator of HSPs) is not the subject of this review per se and this section will concentrate on their activation by cold stress. Transcribing, translating and folding proteins at high temperatures is well known, but cold denaturation of proteins is also documented (Privalov, 1990). For example, the constitutive production of inducible HSP70 is a known feature of polar marine species (Place et al 2004, Clark et al 2008) as a presumed adaptation to life in the cold and the consequential problems of folding proteins at low temperatures.…”

Section: Cold Insect Reviewmentioning

confidence: 99%

How insects survive the cold: molecular mechanisms—a review

2008

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Insects vary considerably in their ability to survive low temperatures. The tractability of these organisms to experimentation has lead to considerable physiology-based work investigating both the variability between species and the actual mechanisms themselves. This has highlighted a range of strategies including freeze tolerance, freeze avoidance, protective dehydration and rapid cold hardening, which are often associated with the production of specific chemicals such as antifreezes and polyol cryoprotectants. But we are still far from identifying the critical elements behind overwintering success and how some species can regularly survive temperatures below -20°C. Molecular biology is the most recent tool to be added to the insect physiologist's armoury. With the public availability of the genome sequence of model insects such as Drosophila and the production of custom-made molecular resources, such as EST libraries and microarrays, we are now in a position to start dissecting the molecular mechanisms behind some of these well-characterised physiological responses. This review aims to provide a state of the art snapshot of the molecular work currently being conducted into insect cold tolerance and the very interesting preliminary results from such studies, which provide great promise for the future.

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“…The process of cold denaturation has been experimentally observed (Privalov, 1990). Consequently, within the framework of this approximate treatment, the native form of a protein is thermodynamically stable over a temperature range Based on these considerations, hyperthermostability can in principle be achieved by some combination of increasing AH, and/or decreasing A S , and/or AC,.…”

Section: Thermodynamic Origins Of Hyperthermostabilitymentioning

confidence: 99%

X‐ray crystal structures of the oxidized and reduced forms of the rubredoxin from the marine hyperthermophilic archaebacterium pyrococcus furiosus

et al. 1992

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The structures of the oxidized and reduced forms of the rubredoxin from the archaebacterium, Pyrococcus furiosus, an organism that grows optimally at 100 °C, have been determined by X‐ray crystallography to a resolution of 1.8 å. Crystals of this rubredoxin grow in space group P212121 with room temperature cell dimensions a = 34.6 å, b = 35.5 å, and c = 44.4 å. Initial phases were determined by the method of molecular replacement using the oxidized form of the rubredoxin from the mesophilic eubacterium, Clostridium pasteurianum, as a starting model. The oxidized and reduced models of P. furiosus rubredoxin each contain 414 nonhydrogen protein atoms comprising 53 residues. The model of the oxidized form contains 61 solvent H2O oxygen atoms and has been refined with X‐PLOR and TNT to a final R = 0.178 with root mean square (rms) deviations from ideality in bond distances and bond angles of 0.014 å and 2.06°, respectively. The model of the reduced form contains 37 solvent H2O oxygen atoms and has been refined to R = 0.193 with rms deviations from ideality in bond lengths of 0.012 å and in bond angles of 1.95°. The overall structure of P. furiosus rubredoxin is similar to the structures of mesophilic rubredoxins, with the exception of a more extensive hydrogen‐bonding network in the β‐sheet region and multiple electrostatic interactions (salt bridge, hydrogen bonds) of the Glu 14 side chain with groups on three other residues (the amino‐terminal nitrogen of Ala 1; the indole nitrogen of Trp 3; and the amide nitrogen group of Phe 29). The influence of these and other features upon the thermostability of the P. furiosus protein is discussed.

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Cold denaturation of myoglobin

Cited by 438 publications

References 37 publications

Firefly luciferase mutants as sensors of proteome stress

Firefly luciferase mutants as sensors of proteome stress

How insects survive the cold: molecular mechanisms—a review

X‐ray crystal structures of the oxidized and reduced forms of the rubredoxin from the marine hyperthermophilic archaebacterium pyrococcus furiosus

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