Sandbox Reserved 199: Difference between revisions
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15N NMR relaxation shows increased T1 values for the residues found in these sheets and loops (0.63-0.64s relative to 0.60s in helices). This suggests greater flexibility in these regions as well. | 15N NMR relaxation shows increased T1 values for the residues found in these sheets and loops (0.63-0.64s relative to 0.60s in helices). This suggests greater flexibility in these regions as well. | ||
[[Image:Kroupa RNase dimer. | [[Image:Kroupa RNase dimer.png|thumb |left |alt=X-Ray Diffraction image. |X-Ray Diffration pattern of a crystallized SARS protease at 2.1 Angstrom resolution.]] | ||
Interestingly, the global correlation time of RNase 1 was shown to be much longer than what is expected for a 13.7 kDa monomer (10ns compared to 6-7ns). This shows that under NMR sample conditions, the RNase1 undergoes dimerization forming a monomer/dimer equilibrium. Because dimerization has shown to have a significant effect on enzyme activity in bovine RNases, certain mutated RNase 1’s which show increased dimerization may be potential anti-cancer therapeutics. | Interestingly, the global correlation time of RNase 1 was shown to be much longer than what is expected for a 13.7 kDa monomer (10ns compared to 6-7ns). This shows that under NMR sample conditions, the RNase1 undergoes dimerization forming a monomer/dimer equilibrium. Because dimerization has shown to have a significant effect on enzyme activity in bovine RNases, certain mutated RNase 1’s which show increased dimerization may be potential anti-cancer therapeutics. | ||
