The Aqueous Interface of a Soluble Protein or the Birth of Epistructural Biology

  • Ariel Fernández Stigliano


For several decades we have witnessed the meteoric development of structural biology. The unraveling of molecular shapes is substantively advancing our understanding of cellular processes. After the pioneering forays in structural biology, we have also seen a veritable deluge of research publications in the related field of molecular biophysics. But this field did not enjoy quite the same level of success as its parental discipline. Despite much effort, the core problems in molecular biophysics continue to challenge researchers. In spite of enticing promises, it is felt that we are nowhere near cracking the protein folding problem from first principles, that we are far from unraveling the physicochemical basis of enzyme catalysis and protein associations, and that we are still unable to engineer therapeutic drugs based on our current understanding of molecular interactions. The acknowledgment of how exquisitely the structure of proteins and their aqueous environment are dynamically entangled attests to the overdue recognition that the biomolecular phenomena cannot be effectively understood without dealing with interfacial behavior. There is an urge to grasp how biological behavior is mediated and affected by the structuring of biomolecular interfaces, in turn determined—somehow—by the structure of proteins. This chapter squarely addresses this imperative and serves as an introduction to a new discipline that we have named epistructural biology. The field may be broadly described as the physicochemical study of the interplay between water and biomolecular structure across the interface. As shown in this chapter, a concept of paramount importance for epistructural biology is the dehydron, a special type of structural defect in soluble proteins recognized as causative of interfacial tension. The role of dehydrons as determinants of the structural and dynamic organization of the aqueous interface will be delineated and the implications for the understanding and control of biomolecular events will be highlighted.


Soluble Protein Disulfide Bond Interfacial Tension Intramolecular Hydrogen Bond Solvation Shell 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


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Copyright information

© Springer International Publishing Switzerland 2015

Authors and Affiliations

  1. 1.National Research Council–CONICETBuenos AiresArgentina
  2. 2.Former Karl F. Hasselmann Endowed Chair Professor of BioengineeringRice UniversityHoustonUSA

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