The explosion of the use of paramagnetic probes to study biological problems by nuclear magnetic resonance (n.m.r.) stems from the large and easily quantifiable perturbations they produce. The main reason for these perturbations is that the magnetic moments of unpaired electrons are about 103 times greater than nuclear magnetic moments and consequently they generate much greater local fields.Such fields can give rise to large shifts in nuclear resonances; but if these fields fluctuate at the appropriate frequencies they will also cause very efficient relaxation in the nuclear resonances. It is possible to select probes that result mainly in one of these parameters being perturbed so that the terms shift and relaxation probe are now well established in the literature.

There is widespread agreement that solar energy is the most promising long-range energy source. However, contemporary technology for bulk energy storage is so primitive that full use of the inevitably erratic solar energy flux is severely limited. Biological systems have perfected methods of storing solar energy for later use in periods of darkness, and it is argued in this symposium presentation that there are many frontiers in biophysics related to the solar energy storage problem. Moreover, the conceivable biological storage systems span a wide range of technology, with appropriate applications in societies of widely varying degrees of industrial development. Use of biological systems to produce hydrogen from solar energy may be among the most versatile of these applications. The entire problem of bioconversion of solar energy presents an excellent example of how the needs for basic scientific understanding and application engineering can be very tightly interwoven.

This review describes recent advances in studies on the stabilities of the three-dimensional structures of proteins and on the processes leading to the formation of these structures. The term ‘protein folding’ will be used here to denote the process of the conversion of an open polypeptide chain into the unique three-dimensional conformation of the native protein. Experimental and theoretical aspects of protein folding have been reviewed by anfinsen & Scheraga (1975). In the present article, we emphasize advances made since the writing of that review, together with a brief summary of the background of recent studies.

The generation of action potentials in nerve and muscle requires cell membranes with steeply voltage-dependent ionic permeabilities. The voltage-dependent, ion-selective pathways responsible for excitation have been characterized for numerous excitable tissues such as nerve axon, muscle, electric organ, algae and epithelia (Aidley, 1971; Hodgkin, 1964; Cole, 1968). The process of activating ionic pathways by some stimulus, such as a change in membrane potential, is called gating.

Proton and carbon-13 nmr spectra of unsonicated lipid bilayers and biological membranes are generally dominated by strong proton–proton and proton–carbon dipolar interactions. As a result the spectra contain a large number of overlapping resonances and are rather difficult to analyse. Nevertheless, important information on the structure and dynamic behaviour of lipid systems has been provided by these techniques (Wennerström & Lindblom, 1977).

The ability of an organism to cope with foreign substances (antigens) depends in part on its capacity to synthesize antibodies (immunoglobulins) of the proper binding specificity to recognize and combine with these antigens. In view of the great variety of possible antigens, antibodies, or more specifically their combining sites, display considerable variation and possess structural properties such as to enable them to bind the antigenic determinants. A vast amount of immunoglobulin sequence data has become available and the three-dimensional structures of a number of immunoglobulin fragments have been elucidated. With these results we can now begin to understand the structural aspects of antibody–antigen reactions. The crystallographic results and the sequence data have been reviewed elsewhere (Capra & Kehoe, 1975; Davies, Padlan & Segal 1975a, b; Gally, 1973; Kabat, 1976; Nisonoff, Hopper & Spring, 1975; Poljak, 1975a, b). Here, an attempt is made to interpret these structural data in terms of the structural evolution of the antibody combining site and the structural basis for the specificity of the binding of antibody to antigen. First, the pertinent crystallographic and sequence data will be presented. Next, the structural studies which reveal the complementarity between antibody and ligand will be described. Then, structural mechanisms by which different combining site structures could be generated will be reviewed.

To talk about enzyme engineering in a context of global problems might seem easy, because the subject is so dynamic and its ramifications so numerous. One might for instance talk about the industrial use of immobilized enzymes to achieve steroid transformations suitable for large-scale production of drugs reducing fertility, or one could describe the application of the same technique for chopping off side-chains of penicillin and other antibiotics as a first step in the production of new semisynthetic drugs, that certainly have a global impact. Or it would be tempting to review the potential of enzyme engineering for synthesizing physiologically active polypeptides that find use in husbandry or medicine.

Small-angle neutron scattering studies of biological macromolecules have developed rapidly in recent years due to the advent of high neutron-flux reactors,† efficient position-sensitive area detectors for neutrons (Allemand et al. 1975) and novel design of instruments (Ibel, 1976). At the same time position-sensitive detectors for X-rays (Gabriel & Dupont, 1972) have revitalized the small-angle X-ray scattering field (Kratky & Pilz, 1972; Luzzati et al. 1976) and it is now becoming clear that neutrons and X-rays can provide complementary structural information on biological complexes.

The form of multicellular animals and their organs is mainly defined by the curvature of cell layers. They are boundaries for solid tissues; and some organs and organisms consist mainly of distinct cell layers (Fig. I a). The form of adult organisms results from a complex interplay of tissue evagination, growth patterns, production of and interaction with extra-cellular material, and other effects; but the rudiments and basic features of the forms produced can often be traced back to processes of evagination or invagination of nearly flat cell sheets at defined locations in the course of embryogenesis.

This review is concerned primarily with the physical structure and changes in the structure of RNA molecules. It will be evident that we have not attempted comprehensive coverage of what amounts to a vast literature. We have tried to stay away from particular areas that have been recently reviewed elsewhere. Citations to and information from them are included, however, so that access to the literature is available. Much of what we treat in depth deals with the crystal structures and solution behaviour of model RNA compounds, including synthetic polymers and molecular fragments such as dinucleoside phosphates. Sequence data on natural RNA are cited, but not in detail. Similarly, apart from tRNA, natural RNAs the structural determinations of which are presently not so far advanced, are not dwelt upon. We have tried to present in detail the available structural data with scaled drawings that permit facile comparisons of molecular geometries.

There is an inherent anisotropy in biological and model membrane systems and this anisotropy has a profound influence on the nuclear magnetic resonance spectra of such systems. For nuclei with a quadrupole moment the quadrupole coupling usually dominates the NMR spectrum, while for nuclei with spin quantum number I = ½ dipolar couplings provides the most important effects. The quadrupole coupling only affects isolated spins and usually gives rise to simple spectra. The dipole interactions on the other hand couple several spins. In a lipid bilayer with a multitude of spin-½ nuclei these couplings can give rise to complicated manybody effects. Thus the interpretation of the NMR spectra of membrane systems poses problems but at the same time there is a lot of information to be gained.