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Contribution of disulfide bonds to stability of the folding intermediate of α-lactalbumin
- Source :
- International Journal of Peptide and Protein Research. 33:289-297
- Publication Year :
- 2009
- Publisher :
- Wiley, 2009.
-
Abstract
- The secondary structure formed in disulfide reduced alpha-lactalbumin is investigated by CD spectrum and is compared with that of the folding intermediate of the disulfide intact protein. The peptide backbone structure of the reduced protein depends strongly on salt concentration in contrast to that of the intermediate. It is close to a random coil in the absence of salt, but it is almost the same as that of the intermediate at a high concentration of salt. The secondary structures of both the proteins undergo broad unfolding transitions when temperature is raised or when urea is added. The secondary structure of the reduced protein is less stable against both heat and urea. These results show that the disulfide bonds are not a determinant of the secondary structure formed at an early stage of folding, and they stabilize the secondary structure of the folding intermediate.
- Subjects :
- Lactalbumin
chemistry.chemical_classification
Protein Conformation
Circular Dichroism
Disulfide bond
Salt (chemistry)
Biochemistry
Random coil
Folding (chemistry)
Kinetics
Crystallography
chemistry.chemical_compound
Drug Stability
chemistry
Urea
Thermodynamics
Spectrophotometry, Ultraviolet
Disulfides
Glycoprotein
Protein secondary structure
Subjects
Details
- ISSN :
- 03678377
- Volume :
- 33
- Database :
- OpenAIRE
- Journal :
- International Journal of Peptide and Protein Research
- Accession number :
- edsair.doi.dedup.....613fd8c7f419eb85c4231816a0f14901