Sandbox Reserved 192: Difference between revisions

RNase A has been used as a foundation enzyme for study due to its stability, small size, and because its three-dimensional structure is fully determined by its amino acid sequence, needing no molecular chaperones. The 1972 Nobel Prize in Chemistry was awarded to three researchers for their work with RNase A on the folding of chains in RNase A and the stability of RNase A. The previously mentioned Christian Anfinsen received the 1972 Nobel Prize in Chemistry for his work on "Principles that govern the folding of protein chains." Stanford Moore and William H. Stein received the 1972 Nobel Prize in Chemistry for their work on "The chemical structures of pancreatic ribonuclease and deoxyribonuclease." The 1984 Nobel Prize in Chemistry was awarded to Robert Bruce Merrifield for his work on "Solid-phase synthesis" using RNase A.    RNase A was the first enzyme and third protein for which its amino acid sequence was correctly determined and the third enzyme and fourth protein whose three-dimensional structure was determined by X-ray diffraction analysis [http://en.wikipedia.org/wiki/X-ray_diffraction_analysis]. Disulfide bonds in RNase A were determined after developing a method using Fast Atom Bombardment Mass Spectrometry (FABMS) [http://en.wikipedia.org/wiki/Fast_atom_bombardment]. The methods of NMR spectroscopy [http://en.wikipedia.org/wiki/NMR_spectroscopy] and Fourier transform infrared (FTIR) spectroscopy [http://en.wikipedia.org/wiki/Fourier_transform_infrared_spectroscopy]  were developed with RNase A in determining protein structure and protein folding pathways. These new methods, developed with RNase A, could be used for further research with other proteins.