PMID: 1958668Nov 26, 1991Paper

Cold denaturation and heat denaturation of Streptomyces subtilisin inhibitor. 1. CD and DSC studies

Biochemistry
A TamuraK Akasaka

Abstract

Cold denaturation and heat denaturation of the protein Streptomyces subtilisin inhibitor (SSI) were studied in the pH range 1.84-3.21 and in the temperature range -3-70 degrees C by circular dichroism and scanning microcalorimetry. The native structure of the protein was apparently most stabilized at about 20 degrees C and was denatured upon heating and cooling from this temperature. Each denaturation was reversible and cooperative, proceeding in two-state transitions, that is, from the native state to the cold-denatured state or from the native state to the heat-denatured state. The two denatured states, however, were not perfect random-coiled structures, and they differed from each other, indicating that there exist three states in this temperature range, i.e., cold denatured, native, and heat denatured. The difference between the cold and heat denaturations was indicated first by circular dichroism. The isodichroic point for the transition from the native state to the cold-denatured state was different from that from the native state to the heat-denatured state in the pH range between 3.21 and 2.45. Moreover, molar ellipticity for the cold-denatured state was different from that of the heat-denatured state, and the transitio...Continue Reading

References

Jan 1, 1989·Annual Review of Biophysics and Biophysical Chemistry·P L Privalov
May 1, 1988·Proceedings of the National Academy of Sciences of the United States of America·Y V Griko Venyaminov SYu
Aug 5, 1986·Journal of Molecular Biology·P L PrivalovV P Kutyshenko

Citations

Apr 1, 1995·Protein Science : a Publication of the Protein Society·K A DillH S Chan
Jul 1, 1995·Protein Science : a Publication of the Protein Society·N N KhechinashviliF Rodier
Oct 23, 1997·Protein Science : a Publication of the Protein Society·T KonnoK Akasaka
Jan 1, 1993·Progress in Biophysics and Molecular Biology·M Oobatake, T Ooi
Jun 1, 2005·Journal of Molecular Biology·Yoshiteru YamadaMasamichi Ikeguchi
May 27, 2004·Journal of the American Chemical Society·Jennifer C TakachAndrew L Feig
Jan 1, 2009·Journal of the American Chemical Society·Monika DavidovicBertil Halle
Aug 16, 2002·European Journal of Biochemistry·T V BurovaCornelus G De Kruif
Sep 17, 2002·European Journal of Biochemistry·Toshihiko KinshoKunio Kimura
Jul 28, 1999·Protein Science : a Publication of the Protein Society·K Sasahara, K Nitta
Nov 29, 2014·The Journal of Chemical Physics·Prathit ChatterjeeNeelanjana Sengupta
Nov 26, 2009·Protein Science : a Publication of the Protein Society·Giovanni BellesiaJoan-Emma Shea
Jan 7, 1998·Journal of Molecular Biology·A Tamura, P L Privalov
Oct 5, 1993·Biochemistry·J M FlanaganD M Engelman
Sep 1, 1996·International Journal of Peptide and Protein Research·E LacassieY Trudelle

Related Concepts

Subtilisin inhibitor protein, Streptomyces
Bacterial Proteins
Calorimetry, Differential Scanning
Circular Dichroism, Vibrational
Cold Temperature
Hydrogen-Ion Concentration
Protein Conformation
Protein Denaturation
Serine Proteinase Inhibitors, Exogenous

Related Feeds

Acute viral rhinopharyngitis

Acute viral rhinopharyngitis, also known as "common cold", is an acute, self-limiting viral infection of the upper respiratory tract involving the nose, sinuses, pharynx and larynx. Discover the latest research on acute viral rhinopharyngitis here.