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Kinetics of amyloid aggregation of mammal apomyoglobins and correlation with their amino acid sequences
- Source :
- FEBS letters. 580(6)
- Publication Year :
- 2006
-
Abstract
- In protein deposition disorders, a normally soluble protein is deposited as insoluble aggregates, referred to as amyloid. The intrinsic effects of specific mutations on the rates of protein aggregation and amyloid formation of unfolded polypeptide chains can be correlated with changes in hydrophobicity, propensity to convert α-helical to β sheet conformation and charge. In this paper, we report the aggregation rates of buffalo, horse and bovine apomyoglobins. The experimental values were compared with the theoretical ones evaluated considering the amino acid differences among the sequences. Our results show that the mutations which play critical roles in the rate-determining step of apomyoglobin aggregation are those located within the N-terminal region of the molecule.
- Subjects :
- Amyloid
Buffaloes
Kinetics
Molecular Sequence Data
Biophysics
Beta sheet
Protein aggregation
Biochemistry
Protein Structure, Secondary
chemistry.chemical_compound
Structural Biology
Genetics
Molecule
Animals
Amino Acid Sequence
Horses
Molecular Biology
chemistry.chemical_classification
Chemistry
Myoglobin
Cell Biology
Amino acid
Protein aggregation rate
Amyloid aggregation
Apomyoglobin aggregation
Cattle
Apoproteins
Subjects
Details
- ISSN :
- 00145793
- Volume :
- 580
- Issue :
- 6
- Database :
- OpenAIRE
- Journal :
- FEBS letters
- Accession number :
- edsair.doi.dedup.....5f57b597abdd4aa53426016c2ab4ca54