Literature DB >> 6712953

Kinetics of cold-induced denaturation of metmyoglobin.

K C Cho, K K Chan.   

Abstract

Using a slow temperature-jump spectrophotometer, we have studied the kinetics of cold-induced denaturation of metmyoglobin between 0 degrees C and 20 degrees C at acidic pH. The time-scale of the transition is slow and is of the order of minutes. The results are consistent with the transition's involving a total of three states, native (N), transient intermediate (I) and denatured (D), which are converted from one to the other in that order.

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Year:  1984        PMID: 6712953     DOI: 10.1016/0167-4838(84)90159-6

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  1 in total

1.  Mapping protein conformational heterogeneity under pressure with site-directed spin labeling and double electron-electron resonance.

Authors:  Michael T Lerch; Zhongyu Yang; Evan K Brooks; Wayne L Hubbell
Journal:  Proc Natl Acad Sci U S A       Date:  2014-03-18       Impact factor: 11.205

  1 in total

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