Other than basic computer skills and having "good hands":
The process of protein folding is one of the most important and challenging research topics of contemporary biochemistry and in spite of its central role in life, it is one of the least understood biophysical processes. In principle, a protein’s final three-dimensional structure and function is dictated by the amino acid sequence. However, proper protein folding into the correct three-dimensional structure is influenced by a number of intracellular factors including biophysical phenomena induced by the polar solvent, molecular chaperones and by specialized macromolecular complexes termed chaperonins.
Errors in protein folding can lead to significant aggregation and severe neurodegenerative disorders such as Alzheimer’s disease, Parkinson’s disease, Huntington’s disease and Amyotrophic lateral sclerosis (ALS). Therefore, it is crucial that we understand the fundamental process of protein folding in order to make significant progress into the treatment of debilitating neurodegenerative disorders.
Computational cryo-EM reconstruction methods, dynamic light scattering (DLS) analysis, protein overexpression and purification, various chromatographic methods for protein purification, protein quantitation and analysis methods, light and electron microscopy, mass spectroscopy and various biochemical and enzymatic activity assays.