Sandbox Reserved 192: Difference between revisions

RNase A has been used as a foundation enzyme for study. 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 also 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. Disulfide bonds in RNase A were determined using Fast Atom Bombardment Mass Spectrometry (FABMS) [http://en.wikipedia.org/wiki/Fast_atom_bombardment]. By mutating the residues of RNase A using site-directed mutagenesis [http://en.wikipedia.org/wiki/Site-directed_mutagenesis], the effects of these mutations were more visibly analyzed with advances in analytical chemistry instrumentation and techniques NMR spectroscopy [http://en.wikipedia.org/wiki/NMR_spectroscopy] and Fourier transform infrared (FTIR) spectroscopy [http://en.wikipedia.org/wiki/Fourier_transform_infrared_spectroscopy] also were used with RNase A to describe protein structure and protein folding.

=='''Further Research'''==

''Replacement of Phe46'': The phenylalanine-46 (<scene name='Sandbox_Reserved_192/Phe_46b/1'>Phe46</scene>) residue located within the hydrophobic core of RNase A was experimentally replaced with other hydrophobic residues; leucine, valine and alanine. The x-ray crystallographic structures were determined in an attempt to conclude how the change would affect the conformational stability. It was concluded that the replacement of Phe46, which is key to the formation of the hydrophobic core, causes the destabilization of the RNase A by preventing the core from being tightly packed. But this has no effect on the substrates ability to bind. The core itself is very limited to adjusting to changes because of its limited mobility from the study di-sulfide bonds