PMID: 3758063Sep 1, 1986Paper

Use of a trypsin-pulse method to study the refolding pathway of ribonuclease

European Journal of Biochemistry
K Lang, F X Schmid

Abstract

Trypsin pulses, applied after varying times of refolding, have been employed to probe the accessibility of the polypeptide chain of ribonuclease A during the process of refolding. The increase in resistance against proteolytic cleavage was measured by activity assays and by sodium dodecyl sulfate/polyacrylamide gel electrophoresis. The sites of cleavage which become inaccessible in the course of refolding are located in the 31 - 39 chain segment of the ribonuclease chain. Protection of this region against attack by trypsin is attained on the major slow refolding pathway in parallel with the formation of a native-like folded, active intermediate, when refolding is carried out under conditions which strongly stabilize the folded state. Under conditions of marginal stability intermediates are not observed during refolding and the formation of trypsin-resistant molecules occurs with the same kinetics as the generation of native ribonuclease. In the native protein the 31 - 39 region of the ribonuclease chain largely forms a loop structure, which is located at the surface of the molecule. Our results indicate that this part of the sequence is still accessible at early stages of refolding, when a hydrogen-bonded network is formed. It ...Continue Reading

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Citations

Apr 1, 1997·Protein Science : a Publication of the Protein Society·P Polverino de LauretoA Fontana
Jan 1, 1987·Progress in Biophysics and Molecular Biology·R Jaenicke
May 1, 1996·European Journal of Biochemistry·U ArnoldR Ulbrich-Hofmann
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Mar 10, 2010·Acta Biochimica Et Biophysica Sinica·Hong-Tao LiYi Liang
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Apr 16, 1998·Biochimica Et Biophysica Acta·S J Hubbard
Jul 1, 1992·Archives of Biochemistry and Biophysics·J M BettonJ M Yon

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