Structural reorganization renders enhanced metalloprotein stability

Claudio Emanuel Gomes

doi:10.1039/c1cc13354c

Structural reorganization renders enhanced metalloprotein stability

Claudio Emanuel Gomes

Instituto de Tecnologia Química e Biológica António Xavier (ITQB)

Research output: Contribution to journal › Article

1 Citation (Scopus)

Abstract

The enhanced stability of a mesophilic metalloprotein was assessed using biophysical spectroscopies. Significant local structural inter-conversions during thermal insult account for a reorganization of the protein scaffold, without disturbing the active metal site. This cushioning mechanism is proposed to be a generic property of metalloproteins contributing to enhanced stability.

Original language	Unknown
Pages (from-to)	11149-11151
Journal	Chemical Communications
Volume	47
Issue number	39
DOIs	https://doi.org/10.1039/c1cc13354c
Publication status	Published - 1 Jan 2011

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10.1039/c1cc13354c

Cite this

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title = "Structural reorganization renders enhanced metalloprotein stability",

abstract = "The enhanced stability of a mesophilic metalloprotein was assessed using biophysical spectroscopies. Significant local structural inter-conversions during thermal insult account for a reorganization of the protein scaffold, without disturbing the active metal site. This cushioning mechanism is proposed to be a generic property of metalloproteins contributing to enhanced stability.",

keywords = "MODEL, DESULFOVIBRIO-GIGAS RUBREDOXIN, CIRCULAR-DICHROISM, MESOPHILIC RUBREDOXIN, PROTEINS, CLOSTRIDIUM-PASTEURIANUM, RESOLUTION, NMR STRUCTURE, DYNAMICS",

author = "Gomes, {Claudio Emanuel}",

year = "2011",

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doi = "10.1039/c1cc13354c",

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AB - The enhanced stability of a mesophilic metalloprotein was assessed using biophysical spectroscopies. Significant local structural inter-conversions during thermal insult account for a reorganization of the protein scaffold, without disturbing the active metal site. This cushioning mechanism is proposed to be a generic property of metalloproteins contributing to enhanced stability.

KW - MODEL

KW - DESULFOVIBRIO-GIGAS RUBREDOXIN

KW - CIRCULAR-DICHROISM

KW - MESOPHILIC RUBREDOXIN

KW - PROTEINS

KW - CLOSTRIDIUM-PASTEURIANUM

KW - RESOLUTION

KW - NMR STRUCTURE

KW - DYNAMICS

U2 - 10.1039/c1cc13354c

DO - 10.1039/c1cc13354c

M3 - Article

VL - 47

SP - 11149

EP - 11151

JO - Chemical Communications

JF - Chemical Communications

SN - 1359-7345

IS - 39

ER -