Back to Search
Start Over
Conformational studies of peptides representing a segment of TM7 from H+-VO-ATPase in SDS micelles
- Source :
- European Biophysics Journal, European Biophysics Journal 39 (2010) 4, European Biophysics Journal, 39(4), 639-646
- Publication Year :
- 2009
- Publisher :
- Springer-Verlag, 2009.
-
Abstract
- The conformation of a transmembrane peptide, sMTM7, encompassing the cytoplasmic hemi-channel domain of the seventh transmembrane section of subunit a from V-ATPase from Saccharomyces cerevisiae solubilized in SDS solutions was studied by circular dichroism (CD) spectroscopy and fluorescence spectroscopy of the single tryptophan residue of this peptide. The results show that the peptide adopts an alpha-helical conformation or aggregated beta-sheet depending on the peptide-to-SDS ratio used. The results are compared with published data about a longer version of the peptide (i.e., MTM7). It is concluded that the bulky, positively charged arginine residue located in the center of both peptides has a destabilizing effect on the helical conformation of the SDS-solubilized peptides, leading to beta-sheet formation and subsequent aggregation.
- Subjects :
- Circular dichroism
Vacuolar Proton-Translocating ATPases
Stereochemistry
Molecular Sequence Data
Biophysics
Peptide
V-ATPase
Saccharomyces cerevisiae
Fluorescence spectroscopy
Protein Structure, Secondary
5th transmembrane segment
nmr
Residue (chemistry)
Aggregation
mimicking
detergent
Secondary structure
Membrane-mimicking solvent
Amino Acid Sequence
Peptide sequence
Protein secondary structure
major coat protein
Spectroscopy
Micelles
chemistry.chemical_classification
proton translocation channel
Original Paper
EPS-2
Protein Stability
Circular Dichroism
Cell Membrane
Tryptophan
Sodium Dodecyl Sulfate
General Medicine
bacteriophage-m13
dodecyl-sulfate micelles
Transmembrane protein
Peptide Fragments
Biofysica
Spectrometry, Fluorescence
chemistry
Biochemistry
Solubility
membrane-proteins
escherichia-coli
SDS micelles
Protein Binding
Subjects
Details
- Language :
- English
- ISSN :
- 14321017 and 01757571
- Volume :
- 39
- Issue :
- 4
- Database :
- OpenAIRE
- Journal :
- European Biophysics Journal
- Accession number :
- edsair.doi.dedup.....4a3f2d973e0301c41b95334212cdb7e8