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Abstract:

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.

Registro:

Documento: Artículo
Título:High pressure reveals structural determinants for globin hexacoordination: neuroglobin and myoglobin cases.
Autor:Capece, L.; Marti, M.A.; Bidon-Chanal, A.; Nadra, A.; Luque, F.J.; Estrin, D.A.
Filiación:Departamento de Química Inorgánica, Analítica y Química Física/ INQUIMAE-CONICET, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Pabellón 2,C1428EHA, Ciudad Universitaria, Buenos Aires, Argentina
Palabras clave: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
Año:2009
Volumen:75
Número:4
Página de inicio:885
Página de fin:894
DOI: http://dx.doi.org/10.1002/prot.22297
Título revista:Proteins
Título revista abreviado:Proteins
ISSN:10970134
CAS:Globins, 9004-22-2; Myoglobin; Nerve Tissue Proteins; neuroglobin
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_10970134_v75_n4_p885_Capece

Citas:

---------- APA ----------
Capece, L., Marti, M.A., Bidon-Chanal, A., Nadra, A., Luque, F.J. & Estrin, D.A. (2009) . High pressure reveals structural determinants for globin hexacoordination: neuroglobin and myoglobin cases. Proteins, 75(4), 885-894.
http://dx.doi.org/10.1002/prot.22297
---------- CHICAGO ----------
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." Proteins 75, no. 4 (2009) : 885-894.
http://dx.doi.org/10.1002/prot.22297
---------- MLA ----------
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." Proteins, vol. 75, no. 4, 2009, pp. 885-894.
http://dx.doi.org/10.1002/prot.22297
---------- VANCOUVER ----------
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. Proteins. 2009;75(4):885-894.
http://dx.doi.org/10.1002/prot.22297