POSTTRANSLATIONAL MODIFICATION OF PROTEINS - COMPLEXITIES OF ANALYSIS OF STRUCTURE AND FUNCTION

The explosion in the development of technologies relating to molecular biology with the simultaneous advances in computer sciences for establishing data bases of DNA and amino acid sequences has led to several interesting controversies concerning research priorities. It is evident that these advances have revolutionized our ability to analyze entire genomes, resulting in the long-awaited diagnosis and treatment of numerous genetic as well as other diseases. However, the proposed time frames predicted for the successes relating to direct as well as indirect applications of these technologies have failed to be realized for several reasons. While it is clear that computer data bases and programs for predicting protein structure have been critical for many studies, to date, the majority of proteins used for these studies are those which have been reasonably simple to purify. Furthermore, it has been reasonably straightforward to crystallize for structure analysis by X-ray crystallography. These current data bases may therefore be limited to these types of proteins, which do not have extensive post-translational modification. There are many modifications of proteins which relate to the physiological roles of proteins in vivo and cause significant alterations, which make them more difficult to purify as well as to predict their biological activities. It is therefore important to develop an appreciation of the potential complexities of protein structures which make them functional. This limited review is provided to give an overview of the complexities for the computational or mathematical oriented investigator who is interested in developing strategies for predicting protein structure from computer data bases.