Protein structure spectroscopic elucidation

It is evident that elucidation of the interfacial behavior of proteins is not a simple matter and requires contributions from several disciplines. In recent years considerable progress has been made in applying spectroscopic techniques to proteins in the adsorbed state (e.g., 7,8,9). In such studies a (small) part of the molecule is analyzed in detail. In our laboratory we study protein adsorption from a more classical, colloid-chemical point of view. Arguments are derived from experimental data referring to whole protein molecules or to layers of them. Information is obtained from adsorption isotherms, proton titrations and both electrokinetic and thermochemical measurements. Recently, topical questions such as reversibility of the adsorption process and changes in the protein structure have been considered. This more holistic approach has produced some insights that could not easily be obtained otherwise. 

The rich spectroscopy and electrochemistry of the heme moiety yields a wealth of opportunities for the denovo heme protein design to evaluate the success of the heme binding site design. Combinations of these spectroscopic and electrochemical methods are elucidating the structure and function of de novo heme proteins and illustrating that they serve as excellent bioinorganic model complexes for simple cytochromes. 

Polymastiamide A (579), an antimicrobial steroid with an unusual side chain modification involving an amide bond to a non-protein amino acid, was isolated from the Norwegian marine sponge Polymastia boletiformis. The structure of polymastiamide A (579) was elucidated by analysis of spectroscopic data and chemical interconversions [470]. Polymastiamides B-F (580-584), additional amino acid conjugates of steroids, were later isolated from the same sponge [471],... 

There are a number of general problems of interest to a bioinorganic chemist that can be addressed by NMR spectroscopy. NMR spectroscopic studies can be instrumental in elucidating the structure of proteins and nucleic acids. The interaction of substrates with cofactors or other cel-... 

---