Macromolecules, transient associations

Water associated with proteins and other macromolecules has traditionally been referred to as bound water. However, to designate such water as bound can be misleading because, for the most part, the water molecules are probably only transiently associated, and at least a portion of the associated water has to be constantly rearranged, due to the thermal perturbations of weak hydrogen bonds. 

Our work aims at identifying, by subpicosecond broadband transient absorption and gain spectroscopy, the primary photochemical steps of the phototransduction process in Blepharisma japonicum, more specifically in the light-adapted form of the organism (blue cell) for which the photoactive pigment is oxyblepharismin [5] (see Scheme 1) and the associated macromolecule is a large non-soluble protein (200 kDa) [6]. 

Macromolecular recognition is ubiquitous in living organisms, and it plays a central role in all biological processes. Proteins specifically interact with other proteins and nucleic acids to form a wide variety of assemblies, from binary complexes to the elaborate multicomponent machines that perform many of the cellular functions.The interaction can be transient, which is the rule in processes such as catalysis or signal transduction, or it can be permanent and build stable assemblies. In either case, it depends on two macromolecules associating to form an interface held by noncovalent forces similar to the forces that stabilize the conformation of the component macromolecules. 

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