An oligopeptide containing the C-terminal sequence of RNase A has a potent RNase A binding property

Journal of the American Chemical Society

Volumn 125, Issue 29, 2003, Pages 8728-8729

  Nakano, Shu Ichi ^a   Sugimoto, Naoki ^a  

^a KONAN UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

OLIGOPEPTIDE; RIBONUCLEASE A;

ARTICLE; BINDING AFFINITY; CARBOXY TERMINAL SEQUENCE; PROTEIN BINDING; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; STRUCTURE ANALYSIS;

AMINO ACID SEQUENCE; FLUORESCENT DYES; KINETICS; MOLECULAR SEQUENCE DATA; OLIGOPEPTIDES; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; RIBONUCLEASE, PANCREATIC; SPECTROPHOTOMETRY;

EID: 0038298132     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja034659r     Document Type: Article

References (25)

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18. All oligopeptides were synthesized on a solid support based on the Fmoc strategy as previously described (Nakano, S.; Sugimoto, N. Bull. Chem. Soc. Jpn. 1998, 71, 2205-2210.). All oligopeptides were confirmed by identification with MALDI-TOF MS (PE Biosystems Voyager).
19. 4 (pH 7.0)/300 mM NaCl. RNase A without lyophilization showed only one peak at 8.8 mL corresponding to the RNase A monomer. The domain-swapped RNase A dimer was prepared as previously reported.
20. The chromatographic analysis for the fraction of the domain-swapped dimers generated no monomer peak, indicating a slow dissociation rate of the dimers. Size exclusion chromatography also showed that lyophilization of RNase A in water gave no oligomeric products.
21. Cole, R.; Loria, J. P. Biochemistry 2002, 41, 6072-6081.
22. The Ala substitution was performed with the histidine corresponding to the acid catalyst in the protein.
23. The titration curve in Figure 3B differs from that in Figure 3A, indicating that the concentrated RNase A and the peptide promoted their association during the lyophilization in water. It also suggests a slow dissociation rate of the peptide from RNase A because both experiments were carried out under the same conditions except for the lyophilization process.
24. The CD spectra also indicated that h(W)β formed a random-coil structure, and the sum of the individual spectrum for h(W)β and RNase A was not the same as that for the equimolar mixture of h(W)β and RNase A.
25. The restoration by β to some extent is consistent with the slight inhibition of the protein dimer by β in Figure 2.