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Physical Biology of Proteins and Peptides pp 153–159Cite as

Dynamics of Membrane Proteins and Lipid Bilayers

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Abstract

Membrane proteins perform relevant physiological functions by means of intricate conformational changes in a hydrophobic environment. Lipid bilayers and embedded proteins, therefore, play a functional role in biomembranes, where the interplay of interactions keeps a delicate balance between cell barriers and selective transducers, transporters, pores, channels, etc. Molecular dynamics and experimental methods (e.g. X-ray diffraction, neutron scattering, nuclear magnetic resonance, infrared spectroscopy, dielectric relaxation spectroscopy, among others) encompass a set of tools to determine the relevant properties that make biomembranes so efficient for preserving life. In this chapter, I provide a perspective on studies that combine experimental methods and molecular dynamics approaches to decipher couplings of membrane proteins and lipid bilayers.

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Notes

  1. 1.

    Analysis performed on trajectories generated by Professor Martin B. Ulmschneider.

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Authors and Affiliations

  1. Departamento de Recursos de la Tierra, Autonomous Metropolitan University (Lerma), Av Hidalgo Poniente No. 46 Col. La Estación, Lerma de Villada, Estado de México, 52006, México

    Héctor Eduardo Jardón-Valadez

Authors
  1. Héctor Eduardo Jardón-Valadez
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Correspondence to Héctor Eduardo Jardón-Valadez .

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Editors and Affiliations

  1. Autonomous University of Mexico City, Mexico City, Distrito Federal, Mexico

    Luis Olivares-Quiroz

  2. (Iztapalapa), Autonomous Metropolitan University, Mexico City, Distrito Federal, Mexico

    Orlando Guzmán-López

  3. (Lerma), Lerma de Villada, Autonomous Metropolitan University, Mexico City, Estado de México, Mexico

    Hector Eduardo Jardón-Valadez

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© 2015 Springer International Publishing Switzerland

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Jardón-Valadez, H.E. (2015). Dynamics of Membrane Proteins and Lipid Bilayers. In: Olivares-Quiroz, L., Guzmán-López, O., Jardón-Valadez, H. (eds) Physical Biology of Proteins and Peptides. Springer, Cham. https://doi.org/10.1007/978-3-319-21687-4_9

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