Conformational studies of equilibrium structures in fragments of horse heart cytochrome c.
Abstract: Ultraviolet absorption and circular dichroism studies have been carried out on horse heart apo-cytochrome c and heme-free peptide fragments obtained by cyanogen bromide cleavage of the native protein. It was noted that the various peptides assume predominantly an unordered conformation in water solution. Increasing ionic strength and addition of 2-chloroethanol increase the right-handed helical content. Guanidinium hydrochloride favors the coil state. It was also demonstrated that two non-interacting helical regions of different stability are present in the apo-protein in 2-chloroethanol.
Publication Date: 1975-01-02 PubMed ID: 165078DOI: 10.1111/j.1432-1033.1975.tb09812.xGoogle Scholar: Lookup
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- Journal Article
Summary
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The research investigates the structural changes in fragments of horse heart cytochrome c when exposed to various conditions. The team used ultraviolet absorption and circular dichroism techniques to observe peptide patterns, finding that the fragments exhibit a largely unordered arrangement in water solution, but increase their helical content with enhanced ionic strength and addition of 2-chloroethanol. The study also identified two non-interacting helical regions in the apo-protein in 2-chloroethanol.
Investigation of Horse Heart Apo-Cytochrome c and Heme-Free Peptide Fragments
- The study explores equilibrium structures in fragments of horse heart cytochrome c using advanced techniques such as ultraviolet (UV) absorption and circular dichroism.
- Upon examining the horse heart apo-cytochrome c and heme-free peptide fragments, the researchers discovered the fragments primarily took on an unordered conformation when in a water solution.
Impact of Ionic Strength and 2-Chloroethanol
- Under different conditions, even larger changes in conformation of the aforementioned fragments were observed.
- When the ionic strength was increased, this led to an increase in the right-handed helical content, representing a significant structural shift.
- Adding 2-chloroethanol, a chemical compound, to the mix also boosted the right-handed helical content further, suggesting that both factors have a profound effect on conformational change.
Effects of Guanidinium Hydrochloride and Presence of Non-Interacting Helical Regions
- The study also introduced guanidinium hydrochloride into the experiment. This substance favored the coil state of the fragments, displaying yet another kind of change in the structure of the fragments.
- Interestingly, when the fragments were immersed in 2-chloroethanol, the apo-protein was found to have two non-interacting helical regions. This shows that the substance can reveal different facets of the protein’s structure.
Cite This Article
APA
Toniolo C, Fontana A, Scoffone E.
(1975).
Conformational studies of equilibrium structures in fragments of horse heart cytochrome c.
Eur J Biochem, 50(2), 367-374.
https://doi.org/10.1111/j.1432-1033.1975.tb09812.x Publication
Researcher Affiliations
MeSH Terms
- Amino Acids / analysis
- Animals
- Binding Sites
- Circular Dichroism
- Cyanogen Bromide
- Cytochrome c Group
- Ethanol / analogs & derivatives
- Guanidines
- Horses
- Myocardium / enzymology
- Osmolar Concentration
- Peptide Fragments / analysis
- Protein Binding
- Protein Conformation
- Spectrophotometry, Ultraviolet
Citations
This article has been cited 2 times.- Polverino de Laureto P, Scaramella E, De Filippis V, Bruix M, Rico M, Fontana A. Limited proteolysis of ribonuclease A with thermolysin in trifluoroethanol.. Protein Sci 1997 Apr;6(4):860-72.
- Solinger AM, Ultee ME, Margoliash E, Schwartz RH. T-lymphocyte response to cytochrome c. I. Demonstration of a T-cell heteroclitic proliferative response and identification of a topographic antigenic determinant on pigeon cytochrome c whose immune recognition requires two complementing major histocompatibility complex-linked immune response genes.. J Exp Med 1979 Oct 1;150(4):830-48.
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