It is generally acknowledged that geometrical and conformational properties of biopolymers have an important effect on their biochemical behaviour. It is less easily recognized that these properties depend also on their macromolecular electronic characteristics.

The aim of this review is to demonstrate the significance of such macromolecular electronic effects. Particularly useful for this sake is the recently much developed concept of ‘molecular electrostatic potential’ (MEP) (Scrocco & Tomasi, 1973, 1978) by which is defined the electrostatic (Coulomb) potential created in the neighbouring space by the nuclear charges and the eletronic distribution of a molecule.

The central points of this paper can now be summarized. We consider here, for simplicity only, vanishing particle concentration. In equilibrium sedimentation equation (6) applies. The density increment is a measurable quantity. It can either be introduced into equation (6) to calculate M2, or it can be analysed by equations (7) and (8) to provide additional information on specific volumes and solute interactions.

Light scattering is determined by the analogous equation (20). The refractive index increment is also experimentally accessible and its structure (not considered here) is similar to that of the density increment. Small angle X-ray scattering is determined by equation (31) and the electron density increment which appears in this equation cannot be directly determined by experiment. Yet it can be obtained in straightforward fashion from the mass density increment, by equation (34). Similarly, in the case of neutron scattering (equation (38)), the scattering length density increment is obtained from the mass density increment by equation (40), or it may now be directly evaluated by neutron interferometry.

Recent progress in membrane biology has brought us to a stage where it is possible to associate complex biological processes to identifiable membrane proteins. Technical advances in the biochemical characterization and purification of membrane proteins have contributed a wealth of structural information. The reconstitution approach has proved to be valuable in our efforts to understand the molecular mechanisms of membrane transport and energy transduction.

Our concern here will be with energetic rather than kinetic aspects of how a macromolecular enzyme molecule or enzyme complex in a biological membrane accomplishes the transfer or transduction of one kind of small-molecule free energy into another. An example is the use of the free energy of ATP hydrolysis (to form ADP and P1) to move Ca2+ across a membrane against its own electrochemical potential gradient (Stryer, 1981). In this case, the free energy decreases in the hydrolysis reaction but much of this is recovered in the form of an increase in free energy of the Ca2+ ions (the remainder is dissipated as heat). There is, of course, no net change in the free energy of the enzyme itself (Ca-ATPase).

Among the Various methods for characterizing macromolecules in solution, hydrodynamic techniques play a major role. Since the advent of the ultracentrifuge and the development of viscometric apparatus, sedimentation coefficients and intrinsic viscosities have been extensively used to learn about the size and shape of synthetic and biological polymers. More recently, refined techniques such as quasielastic light scattering, transient electric birefringence and fluorescence anisotropy decay have made it possible to obtain in a simple and rapid way quantitative information of high precision on the translational and rotational brownian dynamics of dissolved macromolecules.

The apparent and often spectacular movements of animals and insects, movements of the whole organism in relation to its surroundings arising from internally generated forces, have always been, by their very ubiquity, uppermost in our perception of motion in the living world. Movement in plants, generally of one organ in relation to the whole plant, whilst sometimes spectacular, have often in the past been seen as rather esoteric events, amusing perhaps, but of little importance in the general biological scheme of things. However, this is not so; plant movements are quite widespread in occurrence and all are most probably manifestations of a single physiological process, the change in volume of special motor cells. One particular movement, the opening and closing of stomata, which provides a basic control of photosynthesis, is of fundamental importance to the existence of the whole biosphere.

Relaxation techniques have been widely used in kinetic studies of chemical reactions in homogeneous solution (Eigen & DeMayer, 1963). The principle of this method is well known: an external variable such as temperature or pressure is suddenly changed and the time course of a state parameter of the system such as concentration is recorded as it approaches a new steady value. Relaxation techniques can also be used for studying the rate of elementary processes in membranes. This method has proved particularly useful for the investigation of ion transport systems (ion carriers, channels, pumps) in artificial planar bilayer membranes. In this review we describe different relaxation techniques which have been developed for this purpose during the last years, as well as applications to a number of ion transport systems.

In recent years it has become clear that different pathways are involved in the process of removing lesions from DNA. In spite of a continuous surveillance of the genetic integrity by repair enzymes, quite often lesions are not eliminated before the portion of the genome where they have been inserted is used for DNA replication or transcription. Actually, the number of unexcised lesions a cell can tolerate without significantly losing its capacity to reproduce is surprising. As an example, human fibroblasts from certain patients with the genetic disease xeroderma pigmentosum (XP)† are virtually unable to excise pyrimidine dimers, the major DNA lesion produced by short-wavelength UV light.

The spin label method developed by McConnell 15 years ago is now widely used in studies of the structure and dynamic properties of a variety of the biological systems such as proteins and protein complexes, lipids and membranes, nucleic acids, nucleoproteins, etc.

The ESR spectrum of the nitroxide radcal – the spin label – is very sensitive to its microenvironment and permits easy registration of even subtle alterations in it. If spin labels are attached to different sites of a macromolecule the information can be gained about conformational properties of all these local regions and, as a result, about the dynamic behaviour of the object as a whole.

When light impinges on photosynthetic material – a plant leaf, an alga or a photosynthetic bacterium – it is absorbed by an array of lightcollecting pigments. Through resonant energy transfer the absorbed quantum of light is transported to a trap, the reaction centre. Within such a trap, a specialized (bacterio)chlorophyll complex is able to eject from its excited state an electron. This electron is ‘captured’ by an adjacent acceptor, which in turn donates the electron to a second acceptor, and so on. Thus, light energy is converted into chemical energy which is ultimately used in the metabolic processes of the cell.

Isomorphous replacement methods have been revolutionary in macromolecular structure research. This has been most clearly demonstrated in protein crystallography. Specific binding of heavy atoms to protein molecules in the crystalline state provides the necessary reference for the phase determination of each Bragg reflexion and opens the way to the direct structure determination to atomic resolution from X-ray diffraction.

Are isomorphous replacement methods applicable to the investigation of non-crystalline structures as well? And if so, would there be any reasonable advantage?

An answer has been given by neutron scattering. Macromolecular assemblies of nucleic acids, proteins and lipids are most easily studied in H2O /D2O mixtures, as the scattering density of the solvent can be adjusted to any of the chemically different partial structures (Stuhrmann, 1974).