Thermal Stability of Globins: Implications of Flexibility and Heme Coordination Studied by Molecular Dynamics Simulations

Proteins are sensitive to temperature, and abrupt changes in the normal temperature conditions can have a profound impact on both structure and function, leading to protein unfolding. However, the adaptation of certain organisms to extreme conditions raises questions about the structural features th...

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Autores principales: Julió Plana, L., Nadra, A.D., Estrin, D.A., Luque, F.J., Capece, L.
Formato: JOUR
Materias:
Hemoglobin
Molecular dynamics
Porphyrins
Stability
Thermodynamic stability
Classical molecular dynamics
Horse heart myoglobin
Inherent flexibility
Molecular dynamics simulations
Protein thermostabilities
Structural fluctuations
Temperature conditions
Thermal fluctuations
Proteins
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_15499596_v59_n1_p441_JulioPlana
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
id todo:paper_15499596_v59_n1_p441_JulioPlana
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spelling todo:paper_15499596_v59_n1_p441_JulioPlana2023-10-03T16:23:15Z Thermal Stability of Globins: Implications of Flexibility and Heme Coordination Studied by Molecular Dynamics Simulations Julió Plana, L. Nadra, A.D. Estrin, D.A. Luque, F.J. Capece, L. Hemoglobin Molecular dynamics Porphyrins Stability Thermodynamic stability Classical molecular dynamics Horse heart myoglobin Inherent flexibility Molecular dynamics simulations Protein thermostabilities Structural fluctuations Temperature conditions Thermal fluctuations Proteins Proteins are sensitive to temperature, and abrupt changes in the normal temperature conditions can have a profound impact on both structure and function, leading to protein unfolding. However, the adaptation of certain organisms to extreme conditions raises questions about the structural features that permit the structure and function of proteins to be preserved under these adverse conditions. To gain insight into the molecular basis of protein thermostability in the globin family, we have examined three representative examples: human neuroglobin, horse heart myoglobin, and Drosophila hemoglobin, which differ in their melting temperatures and coordination states of the heme iron in the absence of external ligands. In order to elucidate the possible mechanisms that govern the thermostability of these proteins, microsecond-scale classical molecular dynamics simulations were performed at different temperatures. Structural fluctuations and essential dynamics were analyzed, indicating that the flexibility of the CD region, which includes the two short C and D helixes and the connecting CD loop, is directly related to the thermostability. We observed that a larger inherent flexibility of the protein produces higher thermostability, probably concentrating the thermal fluctuations observed at high temperature in flexible regions, preventing unfolding. Globally, the results of this work improve our understanding of thermostability in the globin family. © 2018 American Chemical Society. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_15499596_v59_n1_p441_JulioPlana
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic Hemoglobin
Molecular dynamics
Porphyrins
Stability
Thermodynamic stability
Classical molecular dynamics
Horse heart myoglobin
Inherent flexibility
Molecular dynamics simulations
Protein thermostabilities
Structural fluctuations
Temperature conditions
Thermal fluctuations
Proteins
spellingShingle Hemoglobin
Molecular dynamics
Porphyrins
Stability
Thermodynamic stability
Classical molecular dynamics
Horse heart myoglobin
Inherent flexibility
Molecular dynamics simulations
Protein thermostabilities
Structural fluctuations
Temperature conditions
Thermal fluctuations
Proteins
Julió Plana, L.
Nadra, A.D.
Estrin, D.A.
Luque, F.J.
Capece, L.
Thermal Stability of Globins: Implications of Flexibility and Heme Coordination Studied by Molecular Dynamics Simulations
topic_facet Hemoglobin
Molecular dynamics
Porphyrins
Stability
Thermodynamic stability
Classical molecular dynamics
Horse heart myoglobin
Inherent flexibility
Molecular dynamics simulations
Protein thermostabilities
Structural fluctuations
Temperature conditions
Thermal fluctuations
Proteins
description Proteins are sensitive to temperature, and abrupt changes in the normal temperature conditions can have a profound impact on both structure and function, leading to protein unfolding. However, the adaptation of certain organisms to extreme conditions raises questions about the structural features that permit the structure and function of proteins to be preserved under these adverse conditions. To gain insight into the molecular basis of protein thermostability in the globin family, we have examined three representative examples: human neuroglobin, horse heart myoglobin, and Drosophila hemoglobin, which differ in their melting temperatures and coordination states of the heme iron in the absence of external ligands. In order to elucidate the possible mechanisms that govern the thermostability of these proteins, microsecond-scale classical molecular dynamics simulations were performed at different temperatures. Structural fluctuations and essential dynamics were analyzed, indicating that the flexibility of the CD region, which includes the two short C and D helixes and the connecting CD loop, is directly related to the thermostability. We observed that a larger inherent flexibility of the protein produces higher thermostability, probably concentrating the thermal fluctuations observed at high temperature in flexible regions, preventing unfolding. Globally, the results of this work improve our understanding of thermostability in the globin family. © 2018 American Chemical Society.
format JOUR
author Julió Plana, L.
Nadra, A.D.
Estrin, D.A.
Luque, F.J.
Capece, L.
author_facet Julió Plana, L.
Nadra, A.D.
Estrin, D.A.
Luque, F.J.
Capece, L.
author_sort Julió Plana, L.
title Thermal Stability of Globins: Implications of Flexibility and Heme Coordination Studied by Molecular Dynamics Simulations
title_short Thermal Stability of Globins: Implications of Flexibility and Heme Coordination Studied by Molecular Dynamics Simulations
title_full Thermal Stability of Globins: Implications of Flexibility and Heme Coordination Studied by Molecular Dynamics Simulations
title_fullStr Thermal Stability of Globins: Implications of Flexibility and Heme Coordination Studied by Molecular Dynamics Simulations
title_full_unstemmed Thermal Stability of Globins: Implications of Flexibility and Heme Coordination Studied by Molecular Dynamics Simulations
title_sort thermal stability of globins: implications of flexibility and heme coordination studied by molecular dynamics simulations
url http://hdl.handle.net/20.500.12110/paper_15499596_v59_n1_p441_JulioPlana
work_keys_str_mv AT julioplanal thermalstabilityofglobinsimplicationsofflexibilityandhemecoordinationstudiedbymoleculardynamicssimulations
AT nadraad thermalstabilityofglobinsimplicationsofflexibilityandhemecoordinationstudiedbymoleculardynamicssimulations
AT estrinda thermalstabilityofglobinsimplicationsofflexibilityandhemecoordinationstudiedbymoleculardynamicssimulations
AT luquefj thermalstabilityofglobinsimplicationsofflexibilityandhemecoordinationstudiedbymoleculardynamicssimulations
AT capecel thermalstabilityofglobinsimplicationsofflexibilityandhemecoordinationstudiedbymoleculardynamicssimulations
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