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How conformational flexibility stabilizes the hyperthermophilic elongation factor G-domain

Tutkimustuotosvertaisarvioitu

Standard

How conformational flexibility stabilizes the hyperthermophilic elongation factor G-domain. / Kalimeri, Maria; Rahaman, Obaidur; Melchionna, Simone; Sterpone, Fabio.

julkaisussa: Journal of Physical Chemistry Part B, Vuosikerta 117, Nro 44, 07.11.2013, s. 13775-13785.

Tutkimustuotosvertaisarvioitu

Harvard

Kalimeri, M, Rahaman, O, Melchionna, S & Sterpone, F 2013, 'How conformational flexibility stabilizes the hyperthermophilic elongation factor G-domain', Journal of Physical Chemistry Part B, Vuosikerta. 117, Nro 44, Sivut 13775-13785. https://doi.org/10.1021/jp407078z

APA

Kalimeri, M., Rahaman, O., Melchionna, S., & Sterpone, F. (2013). How conformational flexibility stabilizes the hyperthermophilic elongation factor G-domain. Journal of Physical Chemistry Part B, 117(44), 13775-13785. https://doi.org/10.1021/jp407078z

Vancouver

Kalimeri M, Rahaman O, Melchionna S, Sterpone F. How conformational flexibility stabilizes the hyperthermophilic elongation factor G-domain. Journal of Physical Chemistry Part B. 2013 marras 7;117(44):13775-13785. https://doi.org/10.1021/jp407078z

Author

Kalimeri, Maria ; Rahaman, Obaidur ; Melchionna, Simone ; Sterpone, Fabio. / How conformational flexibility stabilizes the hyperthermophilic elongation factor G-domain. Julkaisussa: Journal of Physical Chemistry Part B. 2013 ; Vuosikerta 117, Nro 44. Sivut 13775-13785.

Bibtex - Lataa

@article{0187f52a7a4d4ba788020d720c018065,
title = "How conformational flexibility stabilizes the hyperthermophilic elongation factor G-domain",
abstract = "Proteins from thermophilic organisms are stable and functional well above ambient temperature. Understanding the molecular mechanism underlying such a resistance is of crucial interest for many technological applications. For some time, thermal stability has been assumed to correlate with high mechanical rigidity of the protein matrix. In this work we address this common belief by carefully studying a pair of homologous G-domain proteins, with their melting temperatures differing by 40 K. To probe the thermal-stability content of the two proteins we use extensive simulations covering the microsecond time range and employ several different indicators to assess the salient features of the conformational landscape and the role of internal fluctuations at ambient condition. At the atomistic level, while the magnitude of fluctuations is comparable, the distribution of flexible and rigid stretches of amino-acids is more regular in the thermophilic protein causing a cage-like correlation of amplitudes along the sequence. This caging effect is suggested to favor stability at high T by confining the mechanical excitations. Moreover, it is found that the thermophilic protein, when folded, visits a higher number of conformational substates than the mesophilic homologue. The entropy associated with the occupation of the different substates and the thermal resilience of the protein intrinsic compressibility provide a qualitative insight on the thermal stability of the thermophilic protein as compared to its mesophilic homologue. Our findings potentially open the route to new strategies in the design of thermostable proteins.",
author = "Maria Kalimeri and Obaidur Rahaman and Simone Melchionna and Fabio Sterpone",
note = "EXT={"}Kalimeri, Maria{"}",
year = "2013",
month = "11",
day = "7",
doi = "10.1021/jp407078z",
language = "English",
volume = "117",
pages = "13775--13785",
journal = "Journal of Physical Chemistry Part B",
issn = "1520-6106",
publisher = "American Chemical Society",
number = "44",

}

RIS (suitable for import to EndNote) - Lataa

TY - JOUR

T1 - How conformational flexibility stabilizes the hyperthermophilic elongation factor G-domain

AU - Kalimeri, Maria

AU - Rahaman, Obaidur

AU - Melchionna, Simone

AU - Sterpone, Fabio

N1 - EXT="Kalimeri, Maria"

PY - 2013/11/7

Y1 - 2013/11/7

N2 - Proteins from thermophilic organisms are stable and functional well above ambient temperature. Understanding the molecular mechanism underlying such a resistance is of crucial interest for many technological applications. For some time, thermal stability has been assumed to correlate with high mechanical rigidity of the protein matrix. In this work we address this common belief by carefully studying a pair of homologous G-domain proteins, with their melting temperatures differing by 40 K. To probe the thermal-stability content of the two proteins we use extensive simulations covering the microsecond time range and employ several different indicators to assess the salient features of the conformational landscape and the role of internal fluctuations at ambient condition. At the atomistic level, while the magnitude of fluctuations is comparable, the distribution of flexible and rigid stretches of amino-acids is more regular in the thermophilic protein causing a cage-like correlation of amplitudes along the sequence. This caging effect is suggested to favor stability at high T by confining the mechanical excitations. Moreover, it is found that the thermophilic protein, when folded, visits a higher number of conformational substates than the mesophilic homologue. The entropy associated with the occupation of the different substates and the thermal resilience of the protein intrinsic compressibility provide a qualitative insight on the thermal stability of the thermophilic protein as compared to its mesophilic homologue. Our findings potentially open the route to new strategies in the design of thermostable proteins.

AB - Proteins from thermophilic organisms are stable and functional well above ambient temperature. Understanding the molecular mechanism underlying such a resistance is of crucial interest for many technological applications. For some time, thermal stability has been assumed to correlate with high mechanical rigidity of the protein matrix. In this work we address this common belief by carefully studying a pair of homologous G-domain proteins, with their melting temperatures differing by 40 K. To probe the thermal-stability content of the two proteins we use extensive simulations covering the microsecond time range and employ several different indicators to assess the salient features of the conformational landscape and the role of internal fluctuations at ambient condition. At the atomistic level, while the magnitude of fluctuations is comparable, the distribution of flexible and rigid stretches of amino-acids is more regular in the thermophilic protein causing a cage-like correlation of amplitudes along the sequence. This caging effect is suggested to favor stability at high T by confining the mechanical excitations. Moreover, it is found that the thermophilic protein, when folded, visits a higher number of conformational substates than the mesophilic homologue. The entropy associated with the occupation of the different substates and the thermal resilience of the protein intrinsic compressibility provide a qualitative insight on the thermal stability of the thermophilic protein as compared to its mesophilic homologue. Our findings potentially open the route to new strategies in the design of thermostable proteins.

UR - http://www.scopus.com/inward/record.url?scp=84887752230&partnerID=8YFLogxK

U2 - 10.1021/jp407078z

DO - 10.1021/jp407078z

M3 - Article

VL - 117

SP - 13775

EP - 13785

JO - Journal of Physical Chemistry Part B

JF - Journal of Physical Chemistry Part B

SN - 1520-6106

IS - 44

ER -