NMR methods for studying protein-protein interactions involved in translation initiation.
Translation in the cell is carried out by complex molecular machinery involving a dynamic network of protein-protein and protein-RNA interactions. Along the multiple steps of the translation pathway, individual interactions are constantly formed, remodeled, and broken, which presents special challenges when studying this sophisticated system. NMR is a still actively developing technology that has recently been used to solve the structures of several translation factors. However, NMR also has a number of other unique capabilities, of which the broader scientific community may not always be aware. In particular, when studying macromolecular interactions, NMR can be used for a wide range of tasks from testing unambiguously whether two molecules interact to solving the structure of the complex. NMR can also provide insights into the dynamics of the molecules, their folding/unfolding, as well as the effects of interactions with binding partners on these processes. In this chapter, we have tried to summarize, in a popular format, the various types of information about macromolecular interactions that can be obtained with NMR. Special attention is given to areas where the use of NMR provides unique information that is difficult to obtain with other approaches. Our intent was to help the general scientific audience become more familiar with the power of NMR, the current status of the technological limitations of individual NMR methods, as well as the numerous applications, in particular for studying protein-protein interactions in translation.
Marintchev
Assen
A
Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts, USA.
Frueh
Dominique
D
Wagner
Gerhard
G
D039642:Eukaryotic Initiation Factors / Q000737:chemistry / Q000378:metabolism; D007553:Isotope Labeling; D046911:Macromolecular Substances; D008957:Models, Genetic; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D010442:Peptide Chain Initiation, Translational; D011485:Protein Binding; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry / Q000378:metabolism
D039642:Eukaryotic Initiation Factors; D046911:Macromolecular Substances; D011506:Proteins