NMR Provides Unique Insight into the Functional Dynamics and
Interactions of Intrinsically Disordered Proteins

J 2022

NMR Provides Unique Insight into the Functional Dynamics and Interactions of Intrinsically Disordered Proteins

CAMACHO-ZARCO, Aldo R., Vincent SCHNAPKA, Serafima GUSEVA, Anton ABYZOV, Wiktor ADAMSKI et. al.

Základní údaje

Originální název

NMR Provides Unique Insight into the Functional Dynamics and Interactions of Intrinsically Disordered Proteins

Autoři

CAMACHO-ZARCO, Aldo R., Vincent SCHNAPKA, Serafima GUSEVA, Anton ABYZOV, Wiktor ADAMSKI, Sigrid MILLES, Malene Ringkjøbing JENSEN, Lukáš ŽÍDEK (203 Česká republika, garant, domácí), Nicola SALVI a Martin BLACKLEDGE

Vydání

CHEMICAL REVIEWS, UNITED STATES, AMER CHEMICAL SOC, 2022, 0009-2665

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10402 Inorganic and nuclear chemistry

Stát vydavatele

Spojené státy

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 62.100

Kód RIV

RIV/00216224:14310/22:00129086

Organizační jednotka

Přírodovědecká fakulta

DOI

http://dx.doi.org/10.1021/acs.chemrev.1c01023

UT WoS

000823421500001

Klíčová slova anglicky

Dynamics; Physical chemistry; Proteins; Reaction kinetics; Thermodynamics

Štítky

rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 19. 8. 2022 12:36, Mgr. Pavla Foltynová, Ph.D.

Anotace

V originále

Intrinsically disordered proteins are ubiquitous throughout all known proteomes, playing essential roles in all aspects of cellular and extracellular biochemistry. To understand their function, it is necessary to determine their structural and dynamic behavior and to describe the physical chemistry of their interaction trajectories. Nuclear magnetic resonance is perfectly adapted to this task, providing ensemble averaged structural and dynamic parameters that report on each assigned resonance in the molecule, unveiling otherwise inaccessible insight into the reaction kinetics and thermodynamics that are essential for function. In this review, we describe recent applications of NMR-based approaches to understanding the conformational energy landscape, the nature and time scales of local and long-range dynamics and how they depend on the environment, even in the cell. Finally, we illustrate the ability of NMR to uncover the mechanistic basis of functional disordered molecular assemblies that are important for human health.

Návaznosti

GA19-12956S, projekt VaV

Název: Klíčové aspekty mykobakteriální transkriprce: SigA, podjednotka RNAP rozpoznávající promotor a její nově identifikovaný vazebný partner.

Investor: Grantová agentura ČR, Klíčové aspekty mykobakteriální transkriprce: SigA, podjednotka RNAP rozpoznávající promotor a její nově identifikovaný vazebný partner.

Citovat

CAMACHO-ZARCO, Aldo R., Vincent SCHNAPKA, Serafima GUSEVA, Anton ABYZOV, Wiktor ADAMSKI, Sigrid MILLES, Malene Ringkjøbing JENSEN, Lukáš ŽÍDEK, Nicola SALVI a Martin BLACKLEDGE. NMR Provides Unique Insight into the Functional Dynamics and Interactions of Intrinsically Disordered Proteins. CHEMICAL REVIEWS. UNITED STATES: AMER CHEMICAL SOC, 2022, roč. 122, č. 10, s. 9331-9356. ISSN 0009-2665. Dostupné z: https://dx.doi.org/10.1021/acs.chemrev.1c01023.

@article{1860349,
   author = {CamachoandZarco, Aldo R. and Schnapka, Vincent and Guseva, Serafima and Abyzov, Anton and Adamski, Wiktor and Milles, Sigrid and Jensen, Malene Ringkjøbing and Žídek, Lukáš and Salvi, Nicola and Blackledge, Martin},
   article_location = {UNITED STATES},
   article_number = {10},
   doi = {http://dx.doi.org/10.1021/acs.chemrev.1c01023},
   keywords = {Dynamics; Physical chemistry; Proteins; Reaction kinetics; Thermodynamics},
   language = {eng},
   issn = {0009-2665},
   journal = {CHEMICAL REVIEWS},
   title = {NMR Provides Unique Insight into the Functional Dynamics and Interactions of Intrinsically Disordered Proteins},
   url = {https://pubs.acs.org/doi/10.1021/acs.chemrev.1c01023},
   volume = {122},
   year = {2022}
}

TY  - JOUR
ID  - 1860349
AU  - Camacho-Zarco, Aldo R. - Schnapka, Vincent - Guseva, Serafima - Abyzov, Anton - Adamski, Wiktor - Milles, Sigrid - Jensen, Malene Ringkjøbing - Žídek, Lukáš - Salvi, Nicola - Blackledge, Martin
PY  - 2022
TI  - NMR Provides Unique Insight into the Functional Dynamics and Interactions of Intrinsically Disordered Proteins
JF  - CHEMICAL REVIEWS
VL  - 122
IS  - 10
SP  - 9331-9356
EP  - 9331-9356
PB  - AMER CHEMICAL SOC
SN  - 00092665
KW  - Dynamics
KW  - Physical chemistry
KW  - Proteins
KW  - Reaction kinetics
KW  - Thermodynamics
UR  - https://pubs.acs.org/doi/10.1021/acs.chemrev.1c01023
N2  - Intrinsically disordered proteins are ubiquitous throughout all known proteomes, playing essential roles in all aspects of cellular and extracellular biochemistry. To understand their function, it is necessary to determine their structural and dynamic behavior and to describe the physical chemistry of their interaction trajectories. Nuclear magnetic resonance is perfectly adapted to this task, providing ensemble averaged structural and dynamic parameters that report on each assigned resonance in the molecule, unveiling otherwise inaccessible insight into the reaction kinetics and thermodynamics that are essential for function. In this review, we describe recent applications of NMR-based approaches to understanding the conformational energy landscape, the nature and time scales of local and long-range dynamics and how they depend on the environment, even in the cell. Finally, we illustrate the ability of NMR to uncover the mechanistic basis of functional disordered molecular assemblies that are important for human health.
ER  -

CAMACHO-ZARCO, Aldo R., Vincent SCHNAPKA, Serafima GUSEVA, Anton ABYZOV, Wiktor ADAMSKI, Sigrid MILLES, Malene Ringkjøbing JENSEN, Lukáš ŽÍDEK, Nicola SALVI a Martin BLACKLEDGE. NMR Provides Unique Insight into the Functional Dynamics and Interactions of Intrinsically Disordered Proteins. \textit{CHEMICAL REVIEWS}. UNITED STATES: AMER CHEMICAL SOC, 2022, roč.~122, č.~10, s.~9331-9356. ISSN~0009-2665. Dostupné z: https://dx.doi.org/10.1021/acs.chemrev.1c01023.

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