Publisher Summary This chapter focuses on protein–protein interaction. The unique characteristics of different proteins are developed in the interactions of proteins with each other, with ions, and with nonprotein materials such as lipids, nucleic acids, and carbohydrates. These range from covalent bonds and electrostatic interactions to the weaker electronic van der Waals' attractive forces characteristic of all atoms and groups of atoms. The interactions of proteins with each other in an aqueous environment may be divided into two categories: (1) those which take place at such distances that the average properties of the protein or its surface may be used in calculating interaction energies, and (2) those in which the interacting molecules approach closely and thus bring into play local forces, the total of which depends to a major extension specific groups and group configurations. Interactions at distances may be further subdivided into those interactions, which lead to a concentration dependence of osmotic pressure, sedimentation coefficient, and those long-range interactions which lead to more complex phenomena such as the separation of phases in suspensions of tobacco mosaic virus and bentonite. An interaction is observed only when the protein molecule is subject to a structural change which brings bonding groups into positions which allow them to interact. Structural changes of this type may be reversible or irreversible. Certain ephemeral interactions, particularly enzymatic reactions, generally lead to chemical or physical changes in one of the interactants to a much greater extent than the other.

Protein-protein interactions.

Micelles. Physical chemistry of surfactant association

From simple micelles in water, nearly spherical aggregates of amphiphilic molecules, to bicontinuous microemulsions, oil and water microheterogeneous mixtures stabilised by a surfactant film with both local and large-scale disordered structures, the world of surfactant-containing systems is fascinating. Depending on a subtle balance of attractive and repulsive interactions between molecules at interfaces, an extraordinarily rich polymorphism of aggregated structures can be observed. After summarising the basic general constraints controlling surfactant aggregation and the formation of interfaces, different structures of micelles and microemulsions are reviewed and related to interfacial film properties and the intermolecular interactions inside them.

https://iopscience.iop.org/article/10.1088/0034-4885/53/3/002/pdf

The structure of micelles and microemulsions

Les etudes cinetiques de l'oxydation des olefines micellaires par des ions permanganate, en solution aqueuse, a 25°C et pH 12, montrent qu'une olefine terminale est oxydee avec une rapidite superieure de 2 ordres que les olefines internes Ce fait est interprete par le desordre et les enroulements rencontres dans la region de Stern riche en eau

On the structure of micelles

Publisher Summary The thrombin-induced conversion of fibrinogen to fibrin that is the primary subject of this review is essentially the final stage in the complex series of processes involved in blood coagulation. Fibrinogen exists in normal blood, while thrombin is present as its precursor prothrombin. The coagulation process consists of the conversion of prothrombin to thrombin and of the subsequent action of thrombin on fibrinogen to produce fibrin. In the fibrinogen-fibrin conversion fibrinogen, already a high polymer of many amino acids is converted to an even higher polymeric form or coagulum, the fibrin clot. Prothrombin can be converted to thrombin in a series of highly complex, and as yet not well understood, reactions. The chapter explores four of the processes by which the conversion of prothrombin to thrombin takes place. These are (1) activation by citrate, (2) activation by calcium ions, Ac-globulin and thromboplastin, (3) activation by calcium ions, platelets and thromboplastin, and (4) activation by trypsin. The chapter concludes by addressing the various problems of current interest in protein chemistry, which appear in the study of the fibrinogen-fibrin conversion. The first step is an example of a limited proteolysis by a protease of curious specificity. This proteolysis may turn out to be one of the first illustrations of the existence of “strong” peptide bonds in proteins. Further, it offers a nice illustration of the phenomenon of unmasking or activation in biological systems. The second step involves protein-protein associations with unequal association constants. The last step may involve gel formation or crystallization.

The Fibrinogen-Fibrin Conversion1

Flow Birefringence in Solutions of n-Hexadecyltrimethylammonium Bromide1,2

Flow Birefringence in Arrested Clotting Systems1

Dynamo-optical properties of detergent micelles

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Flow Birefringence in Solutions of n-Hexadecyltrimethylammonium Bromide1,2

Flow Birefringence in Arrested Clotting Systems1

Dynamo-optical properties of detergent micelles