Inspired by the recent progress in NMR spectroscopy we have worked on methods to recognize protein folds, large conformational changes as well as on means to build models of oligomers and quaternary complexes. We make use of transverse relaxation optimized NMR spectroscopy in measurements from weakly aligned systems and data available from small angle scattering of x-rays. We expect that combining these solution state methods to employ known high-resolution subunit structures rather to explicitly determine modular structures will become more and more useful as the protein data bank grows larger in its diversity due to progress in structural genomics. The novel methods will serve to gain understanding in questions of structure - function relationships and in applications of drug discovery and protein engineering e.g. by screening ligands, leads and mutations.