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Updated: Jun 27, 2026
04:37
High-Pressure NMR Experiments for Detecting Protein Low-Lying Conformational States
Published on: June 29, 2021
High pressure reveals structural determinants for globin hexacoordination: neuroglobin and myoglobin cases
L Capece1, M A Marti, A Bidon-Chanal
1Departamento de Química Inorgánica, Analítica y Química Física/ INQUIMAE-CONICET, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Ciudad Universitaria, Pabellón 2, Buenos Aires, C1428EHA Argentina.
Proteins
|December 18, 2008
Summary
High pressure reduces protein mobility but enhances hexacoordination in neuroglobin (Ngb) and myoglobin (Mb). The C-D region
Area of Science:
- Biophysics
- Computational Biology
- Structural Biology
Background:
- Neuroglobin (Ngb) and myoglobin (Mb) are key proteins involved in oxygen transport and storage.
- Understanding protein coordination states is crucial for elucidating their function.
- Pressure is a significant environmental factor influencing protein dynamics and equilibria.
Purpose of the Study:
- To investigate the influence of pressure on the five-coordination (5c) and six-coordination (6c) states in Ngb and Mb.
- To elucidate the role of protein structure and dynamics in controlling the 5c/6c equilibrium under pressure.
- To compare the pressure-induced effects on hexacoordination in Ngb and Mb.
Main Methods:
- Molecular dynamics (MD) simulations were employed to study Ngb and Mb at normal and high pressures.
- Steered MD simulations were used to obtain free energy profiles for coordination state transitions.
- Analysis focused on protein mobility, structural changes, and the dynamics of specific protein regions like the C-D region.
Main Results:
- High pressure significantly reduces protein mobility in both Ngb and Mb without causing major structural alterations.
- The equilibrium between 5c and 6c states is predominantly governed by the structure and dynamics of the C-D region.
- High pressure was found to enhance hexacoordination in both proteins, consistent with experimental data.
Conclusions:
- Pressure-induced changes in protein dynamics, particularly in the C-D region, are key to modulating the 5c/6c equilibrium in globins.
- In Ngb, enhanced hexacoordination is attributed to an increased transition barrier from 6c to 5c.
- In Mb, the shift towards hexacoordination is primarily driven by the destabilization of the 5c state under high pressure.
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