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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todo:paper_10970134_v75_n4_p885_Capece2023-10-03T16:05:26Z High pressure reveals structural determinants for globin hexacoordination: neuroglobin and myoglobin cases. Capece, L. Marti, M.A. Bidon-Chanal, A. Nadra, A. Luque, F.J. Estrin, D.A. 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. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar 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, L. Marti, M.A. Bidon-Chanal, A. Nadra, A. Luque, F.J. Estrin, D.A. 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. |
format |
JOUR |
author |
Capece, L. Marti, M.A. Bidon-Chanal, A. Nadra, A. Luque, F.J. Estrin, D.A. |
author_facet |
Capece, L. Marti, M.A. Bidon-Chanal, A. Nadra, A. Luque, F.J. Estrin, D.A. |
author_sort |
Capece, L. |
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. |
url |
http://hdl.handle.net/20.500.12110/paper_10970134_v75_n4_p885_Capece |
work_keys_str_mv |
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