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primary topic: Partial destabilization of native structure by a combination of heat and denaturant facilitates cold denaturation in a hyperthermophile protein.

Partial destabilization of native structure by a combination of heat and denaturant facilitates cold denaturation in a hyperthermophile protein.
type: AcademicArticle
type: Article
abstract: Cold denaturation is a phenomenon seen in many different proteins. However, there have been no reports so far of its occurrence in hyperthermophile proteins. Here, using a recombinant triosephosphate isomerase (PfuTIM) from the hyperthermophile archaeon, Pyrococcus furiosus, we show that the heating of this protein through the low temperature side of its thermal unfolding transition in the presence of guanidinium hydrochloride (GdmCl) results in the formation of partially-disordered conformational ensembles that retain considerable native-like secondary and tertiary structure. Unlike PfuTIM itself, these thermochemically obtained partially-disordered PfuTIM ensembles display cold denaturation as they are cooled to room temperature. The protein thus shows hysteresis, adopting different structural states in a manner dependent upon the nature of the heating and cooling treatment, rather than upon the initial and final conditions of temperature and GdmCl concentration, indicating that some sort of a kinetic effect influences structure adoption and retention. The structure lost through cooling of partially-disordered PfuTIM is found to be regained through heating. The ability of GdmCl to thus apparently destabilize the highly thermodynamically and kinetically stable structure of PfuTIM (sufficiently, to cause it to display observable cold-denaturation and heat-renaturation transitions, in real-time, with cooling and heating) offers support to current ideas concerning the how hyperthermophile proteins achieve their high kinetic stabilities, and suggests that desolvation-solvation barriers may be responsible for high kinetic stability.
date: 2008-08
volume: 72
issue: 2
is part of: Proteins
status: peerReviewed
status: published
author list: authors
type: EPrint
type: ArticleEPrint
is part of: repository
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subject: QR Microbiology

Partial destabilization of native structure by a combination of heat and denaturant facilitates cold denaturation in a hyperthermophile protein. (PDF)
type: Document

Wiley
type: Organization

Proteins
type: Collection
issn: 10970134

Purnananda Guptasarma
type: Person
given name: Purnananda
family name: Guptasarma

Sanjeev Kumar Chandrayan
type: Person
given name: Sanjeev Kumar
family name: Chandrayan

Partial destabilization of native structure by a combination of heat and denaturant facilitates cold denaturation in a hyperthermophile protein. (Image (PNG))
type: Document
is version of: Partial destabilization of native structure by a combination of heat and denaturant facilitates cold denaturation in a hyperthermophile protein. (PDF)
is volatile version of: Partial destabilization of native structure by a combination of heat and denaturant facilitates cold denaturation in a hyperthermophile protein. (PDF)
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Partial destabilization of native structure by a combination of heat and denaturant facilitates cold denaturation in a hyperthermophile protein. (Image (PNG))
type: Document
is version of: Partial destabilization of native structure by a combination of heat and denaturant facilitates cold denaturation in a hyperthermophile protein. (PDF)
is volatile version of: Partial destabilization of native structure by a combination of heat and denaturant facilitates cold denaturation in a hyperthermophile protein. (PDF)
ispreview thumbnail version of: Partial destabilization of native structure by a combination of heat and denaturant facilitates cold denaturation in a hyperthermophile protein. (PDF)

Partial destabilization of native structure by a combination of heat and denaturant facilitates cold denaturation in a hyperthermophile protein. (Image (PNG))
type: Document
is version of: Partial destabilization of native structure by a combination of heat and denaturant facilitates cold denaturation in a hyperthermophile protein. (PDF)
is volatile version of: Partial destabilization of native structure by a combination of heat and denaturant facilitates cold denaturation in a hyperthermophile protein. (PDF)
ismedium thumbnail version of: Partial destabilization of native structure by a combination of heat and denaturant facilitates cold denaturation in a hyperthermophile protein. (PDF)

Partial destabilization of native structure by a combination of heat and denaturant facilitates cold denaturation in a hyperthermophile protein. (Image (PNG))
type: Document
is version of: Partial destabilization of native structure by a combination of heat and denaturant facilitates cold denaturation in a hyperthermophile protein. (PDF)
is volatile version of: Partial destabilization of native structure by a combination of heat and denaturant facilitates cold denaturation in a hyperthermophile protein. (PDF)
issmall thumbnail version of: Partial destabilization of native structure by a combination of heat and denaturant facilitates cold denaturation in a hyperthermophile protein. (PDF)

Partial destabilization of native structure by a combination of heat and denaturant facilitates cold denaturation in a hyperthermophile protein. (Indexer Terms)
type: Document
is version of: Partial destabilization of native structure by a combination of heat and denaturant facilitates cold denaturation in a hyperthermophile protein. (PDF)
is volatile version of: Partial destabilization of native structure by a combination of heat and denaturant facilitates cold denaturation in a hyperthermophile protein. (PDF)
is index codes version of: Partial destabilization of native structure by a combination of heat and denaturant facilitates cold denaturation in a hyperthermophile protein. (PDF)

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primary topic: Partial destabilization of native structure by a combination of heat and denaturant facilitates cold denaturation in a hyperthermophile protein.

QR Microbiology
type: Concept