Paper del nucli hidrofòbic principal de la RNasa A en el plegament i desplegament induïts per pressió i temperatura
作者： Josep Font i Sadurní
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摘要: EnglishUsing temperature and pressure as denaturants we have explored the contributions to stability of hydrophobic core residues RNase A. These results are consistent with an exquisite tight packing existence rearrangements in protein interior. The role interactions established by main A its pressure-folding transition state, was investigated using ?-value method. Altogether suggest that state A, looks like a collapsed globule some secondary structure weakened core. Pressure-jump induced relaxation kinetics used explore energy landscape folding/unfolding Y115W variant appears interact strongly hydration shell, indicated presence glycerol. catalaUtilitzant temperatura i pressio com agents desnaturalitzants sha explorat la contribucio lestabilitat de diferents residus del principal nucli hidrofobic RNasa Aquests resutats suggereixen que el daquest enzim, esta fortament empaquetat ha revelat lexistencia reordenacions en linterior proteina. El metode dels valors ?, han permes estudiar paper les interaccions hidrofobiques establertes pels seu estat transicio induit per pressio. En conjunt, aquests resultats lestat sassemblaria un globul collapsat amb una cadena estructurada pero debilitat hidrofobic. Sha tambe, paisatge energetic plegament/desplegament proteic Lestat sembla interaccionar capa dhidratacio estat, tal indiquen els presencia glicerol.
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