Identification of Posttranslational Modification Sites by Site-Directed Mutagenesis
Following translation, many proteins undergo further modifications that can dramatically affect both their physical properties and biological function (Wold and Moldave, 1984; Freedman and Hawkins, 1985; Harding and Crabbe, 1992). These posttranslational modifications are essential to the vitality of all eukaryotic cells, including neurons. Techniques that identify amino acid residues in a given protein that are modified and assess the effect of eliminating a specific modification site on a protein’s function, both in vitro or in the context of cellular expression, are useful in studying posttranslational modifications. The more traditional biochemical and immunological methods of studying posttranslational modification are discussed elsewhere in this book. However, the resources required for these approaches may not always be available or may yield equivocal results. Thus, the powerful tools of molecular biology may provide a viable alternative for identifying sites of posttranslational modification.
- Alternative Pre-mRNA Splicing of G Protein-Coupled Receptors
- A Infusion and Related Models of Alzheimer Dementia
- Hybrid Neuronal Network Studies Under Dynamic Clamp
- The Role of Calpain in Neurofilament Protein Degradation Associated With Spinal Cord Injury
- Juxtacellular Neuronal Labelling, Physiological Characterization and Phenotypic Identification of Single Neurons In Vivo
- Use of Affinity Chromatography in Purification of A1 Adenosine Receptors from Rat Brain Membranes
- Spontaneous Rhythmic Activity in the Adult Cerebral Cortex In Vitro
- Application of Zymographic Methods to Study Matrix Enzymes Following Traumatic Brain Injury
- DISC1 Mouse Models
- Axonal Transport Methods and Applications