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Use of vector formalism in the analysis of hydrophobic and electric driving forces in biological assemblies

Published online by Cambridge University Press:  11 April 2022

Angel Mozo-Villarías Open the ORCID record for Angel Mozo-Villarías [Opens in a new window] ,
Juan A. Cedano Open the ORCID record for Juan A. Cedano [Opens in a new window]  and
Enrique Querol Open the ORCID record for Enrique Querol [Opens in a new window]
Angel Mozo-Villarías*
Affiliation:
Institut de Biotecnologia i Biomedicina and Departament de Bioquímica i Biologia Molecular, Campus de Bellaterra, Universitat Autónoma de Barcelona, 08193 Bellaterra, Barcelona, Spain
Juan A. Cedano
Affiliation:
Institut de Biotecnologia i Biomedicina and Departament de Bioquímica i Biologia Molecular, Campus de Bellaterra, Universitat Autónoma de Barcelona, 08193 Bellaterra, Barcelona, Spain
Enrique Querol
Affiliation:
Institut de Biotecnologia i Biomedicina and Departament de Bioquímica i Biologia Molecular, Campus de Bellaterra, Universitat Autónoma de Barcelona, 08193 Bellaterra, Barcelona, Spain
*
Author for correspondence: Angel Mozo-Villarías, E-mail: angel.mozo@mex.udl.cat
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Abstract

Hydrophobic forces are known to have a crucial part not only in the conformation of the three-dimensional structure of proteins, but also in the build-up of DNA–protein complexes. Electric forces also play an important role both in the tertiary as well in the quaternary structure of macromolecular associations. Sometimes both hydrophobic and electric interactions add up their strengths to accomplish these structures but in most cases they act in opposite directions. This fact, together with being overall interactions with different ranges, provides a nuanced equilibrium also modulated by the need to comply with steric hindrances and geometric frustration effects. This review focuses on the utility of using the hydrophobic and electrical dipole moment vectors to describe the interactions that give rise to the structures of biological macromolecules. Although different definitions of both electric dipole and hydrophobic moments have been described in the literature, results obtained in biological assemblies demonstrate the principle of the biological membrane model. According to this model, postulated by our group, biological macromolecules tend to associate by aligning their hydrophobic moments in a similar manner to phospholipids in a membrane. Examples of both closed and open structures are used to assess the predictability of our model. We seek agreement between our results with those described in the current literature. The review ends with possible future projections using this formalism.

Keywords

Biological membrane modelconsensus DNADNAelectric dipole momenthydrophobic energyhydrophobic interactionhydrophobic momentproteinsprotein self-assemblingtranscription systems
Type
Review Article
Information
Quarterly Reviews of Biophysics , Volume 55 , 2022 , e4
Copyright
Copyright © The Author(s), 2022. Published by Cambridge University Press

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