Circular dichroism study of ribonuclease A mutants containing the minimal structural requirements for dimerization and swapping
作者： Francesca Catanzano , Giuseppe Graziano , Valeria Cafaro , Giuseppe D’Alessio , Alberto Di Donato
DOI: 10.1016/S0141-8130(98)00060-9
关键词: RNase P 、 Protein stability 、 Ribonuclease 、 Protein structure 、 Thermal denaturation 、 Bovine seminal ribonuclease 、 Crystallography 、 Mutant 、 Chemistry 、 Circular dichroism
摘要: Abstract Four residues Pro19, Leu28, Cys31 and Cys32 proved to be the minimal structural requirements in determining dimeric structure N-terminal segment swapping of bovine seminal ribonuclease, BS-RNase. We analyzed content secondary tertiary structures RNase A, P-RNase PL-RNase MCAM-PLCC-RNase A MCAM-BS-RNase, performing near far-UV CD spectra. It results that five proteins have very similar native conformations. Thermal denaturation at pH 5.0 proteins, studied by means measurements, reversible well represented two-state N⇔D transition model. Thermodynamic data are discussed light information available for
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