toggle visibility Search & Display Options

Select All    Deselect All
 |   | 
  Record Links
Author (up) Tsong, T.Y. openurl 
  Title Conformational relaxations of urea- and guanidine hydrochloride-unfolded ferricytochrome c Type Journal Article
  Year 1977 Publication The Journal of Biological Chemistry Abbreviated Journal J Biol Chem  
  Volume 252 Issue 24 Pages 8778-8780  
  Keywords *Cytochrome c Group; Guanidines/*pharmacology; Protein Conformation/drug effects; Spectrometry, Fluorescence; Urea/*pharmacology  
  Abstract Several recent studies of protein the unfolded proteins. In urea- and guanidine HCl-unfolded ferricytochrome c (horse heart), an acid-induced spin state transformation of the heme group has been detected by the heme absorptions, Trp-59 fluorescence, and the intrinsic viscosity of protein. Kinetics of this second conformational transition, by the temperature jump and stopped flow methods, are complex. One rapid reaction (tau1), pH-independent, occurs in a 50-mus range; the second reaction (tau2), in a 1-ms range, depends linearly upon pH and is faster at the alkaline side; a third reaction (tau3), in a 1-s range, shows a sigmoidal transition at pH 5.1 and is faster at the acidic side. The results are consistent with a kinetic scheme which involves protein conformational changes in the transformation of the heme coordination state. The kinetics, along with previous equilibrium studies, indicate that ligand or charge interactions within a protein molecule are not completely prohibited even in strongly denaturing conditions, such as in high concentrations of urea and guanidine HCl. Thus, local structures of peptide chain associated with these interactions can exist in the unfolded protein.  
  Corporate Author Thesis  
  Publisher Place of Publication Editor  
  Language English Summary Language Original Title  
  Series Editor Series Title Abbreviated Series Title  
  Series Volume Series Issue Edition  
  ISSN 0021-9258 ISBN Medium  
  Area Expedition Conference  
  Notes PMID:200618 Approved no  
  Call Number refbase @ user @ Serial 3882  
Permanent link to this record
Select All    Deselect All
 |   |