High pressure reveals structural determinants for globin hexacoordination: neuroglobin and myoglobin cases.

The influence of pressure on the equilibrium between five-(5c) and six-coordination (6c) forms in neuroglobin (Ngb) and myoglobin (Mb) has been examined by means of molecular dynamics (MD) simulations at normal and high pressure. The results show that the main effect of high pressure is to reduce th...

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Autores principales:	Capece, Luciana, Martí, Marcelo Adrián, Nadra, Alejandro Daniel, Estrin, Dario Ariel
Publicado:	2009
Materias:	globin myoglobin nerve protein neuroglobin animal article chemical structure chemistry computer simulation entropy human mouse pressure protein conformation protein tertiary structure statistical analysis thermodynamics Animals Computer Simulation Data Interpretation, Statistical Entropy Globins Humans Mice Models, Molecular Myoglobin Nerve Tissue Proteins Pressure Protein Conformation Protein Structure, Tertiary Thermodynamics
Acceso en línea:	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_10970134_v75_n4_p885_Capece http://hdl.handle.net/20.500.12110/paper_10970134_v75_n4_p885_Capece
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	paper:paper_10970134_v75_n4_p885_Capece
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spelling	paper:paper_10970134_v75_n4_p885_Capece2023-06-08T16:07:05Z High pressure reveals structural determinants for globin hexacoordination: neuroglobin and myoglobin cases. Capece, Luciana Martí, Marcelo Adrián Nadra, Alejandro Daniel Estrin, Dario Ariel globin myoglobin nerve protein neuroglobin animal article chemical structure chemistry computer simulation entropy human mouse pressure protein conformation protein tertiary structure statistical analysis thermodynamics Animals Computer Simulation Data Interpretation, Statistical Entropy Globins Humans Mice Models, Molecular Myoglobin Nerve Tissue Proteins Pressure Protein Conformation Protein Structure, Tertiary Thermodynamics The influence of pressure on the equilibrium between five-(5c) and six-coordination (6c) forms in neuroglobin (Ngb) and myoglobin (Mb) has been examined by means of molecular dynamics (MD) simulations at normal and high pressure. The results show that the main effect of high pressure is to reduce the protein mobility without altering the structure in a significant manner. Moreover, our data suggest that the equilibrium between 5c and 6c states in globins is largely controlled by the structure and dynamics of the C-D region. Finally, in agreement with the available experimental data, the free energy profiles obtained from steered MD for both proteins indicate that high pressure enhances hexacoordination. In Ngb, the shift in equilibrium is mainly related to an increase in the 6c-->5c transition barrier, whereas in Mb such a shift is primarily due to a destabilization of the 5c state. Copyright 2008 Wiley-Liss, Inc. Fil:Capece, L. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Marti, M.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Nadra, A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Estrin, D.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 2009 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_10970134_v75_n4_p885_Capece http://hdl.handle.net/20.500.12110/paper_10970134_v75_n4_p885_Capece
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-134
collection	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic	globin myoglobin nerve protein neuroglobin animal article chemical structure chemistry computer simulation entropy human mouse pressure protein conformation protein tertiary structure statistical analysis thermodynamics Animals Computer Simulation Data Interpretation, Statistical Entropy Globins Humans Mice Models, Molecular Myoglobin Nerve Tissue Proteins Pressure Protein Conformation Protein Structure, Tertiary Thermodynamics
spellingShingle	globin myoglobin nerve protein neuroglobin animal article chemical structure chemistry computer simulation entropy human mouse pressure protein conformation protein tertiary structure statistical analysis thermodynamics Animals Computer Simulation Data Interpretation, Statistical Entropy Globins Humans Mice Models, Molecular Myoglobin Nerve Tissue Proteins Pressure Protein Conformation Protein Structure, Tertiary Thermodynamics Capece, Luciana Martí, Marcelo Adrián Nadra, Alejandro Daniel Estrin, Dario Ariel High pressure reveals structural determinants for globin hexacoordination: neuroglobin and myoglobin cases.
topic_facet	globin myoglobin nerve protein neuroglobin animal article chemical structure chemistry computer simulation entropy human mouse pressure protein conformation protein tertiary structure statistical analysis thermodynamics Animals Computer Simulation Data Interpretation, Statistical Entropy Globins Humans Mice Models, Molecular Myoglobin Nerve Tissue Proteins Pressure Protein Conformation Protein Structure, Tertiary Thermodynamics
description	The influence of pressure on the equilibrium between five-(5c) and six-coordination (6c) forms in neuroglobin (Ngb) and myoglobin (Mb) has been examined by means of molecular dynamics (MD) simulations at normal and high pressure. The results show that the main effect of high pressure is to reduce the protein mobility without altering the structure in a significant manner. Moreover, our data suggest that the equilibrium between 5c and 6c states in globins is largely controlled by the structure and dynamics of the C-D region. Finally, in agreement with the available experimental data, the free energy profiles obtained from steered MD for both proteins indicate that high pressure enhances hexacoordination. In Ngb, the shift in equilibrium is mainly related to an increase in the 6c-->5c transition barrier, whereas in Mb such a shift is primarily due to a destabilization of the 5c state. Copyright 2008 Wiley-Liss, Inc.
author	Capece, Luciana Martí, Marcelo Adrián Nadra, Alejandro Daniel Estrin, Dario Ariel
author_facet	Capece, Luciana Martí, Marcelo Adrián Nadra, Alejandro Daniel Estrin, Dario Ariel
author_sort	Capece, Luciana
title	High pressure reveals structural determinants for globin hexacoordination: neuroglobin and myoglobin cases.
title_short	High pressure reveals structural determinants for globin hexacoordination: neuroglobin and myoglobin cases.
title_full	High pressure reveals structural determinants for globin hexacoordination: neuroglobin and myoglobin cases.
title_fullStr	High pressure reveals structural determinants for globin hexacoordination: neuroglobin and myoglobin cases.
title_full_unstemmed	High pressure reveals structural determinants for globin hexacoordination: neuroglobin and myoglobin cases.
title_sort	high pressure reveals structural determinants for globin hexacoordination: neuroglobin and myoglobin cases.
publishDate	2009
url	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_10970134_v75_n4_p885_Capece http://hdl.handle.net/20.500.12110/paper_10970134_v75_n4_p885_Capece
work_keys_str_mv	AT capeceluciana highpressurerevealsstructuraldeterminantsforglobinhexacoordinationneuroglobinandmyoglobincases AT martimarceloadrian highpressurerevealsstructuraldeterminantsforglobinhexacoordinationneuroglobinandmyoglobincases AT nadraalejandrodaniel highpressurerevealsstructuraldeterminantsforglobinhexacoordinationneuroglobinandmyoglobincases AT estrindarioariel highpressurerevealsstructuraldeterminantsforglobinhexacoordinationneuroglobinandmyoglobincases
_version_	1768546128759881728

High pressure reveals structural determinants for globin hexacoordination: neuroglobin and myoglobin cases.

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