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Disordered N-terminal residues affect the folding thermodynamics and kinetics of maltose binding protein
- Source :
- FEBS Letters. (3):307-311
- Publisher :
- Published by Elsevier B.V.
-
Abstract
- Maltose binding protein (MBP) exhibits a slow phase of folding at pH 7.4, 298 K. The kinetics of this phase has been characterized as a function of denaturant concentration and temperature. Denaturant double-jump experiments and the activation energy for folding indicate that the slow phase involves processes other than proline isomerization. Although the first five N-terminal residues are disordered in the MBP crystal structure, mutations in this region slow down folding and destabilize the native structure. This is the first report showing that disordered N-terminal residues can affect folding kinetics and stability.
- Subjects :
- Protein Folding
pm, periplasmic mature protein
ΔG, free energy change
Monosaccharide Transport Proteins
Kinetics
u, unfolding
Biophysics
Biochemistry
Maltose-Binding Proteins
Maltose-binding protein
Bacterial Proteins
Structural Biology
Phase (matter)
Genetics
Escherichia coli
TOF, time of flight
k, rate constant
Proline
MALDI, matrix assisted laser desorption ionization
Molecular Biology
cm cytoplasmic mature protein
f, folding
Ea, activation barrier
Cm, denaturant concentration at which half the molecules are unfolded
biology
Double jump
Mass spectrometry
ESI, electrospray ionization
Chemistry
Escherichia coli Proteins
Folding
Cell Biology
CGH, equimolar citrate-glycine-HEPES
Maltose binding protein
Folding (chemistry)
MS, mass spectrometry
LA, lactalbumin
MBP, maltose binding protein
biology.protein
Thermodynamics
Protein folding
ATP-Binding Cassette Transporters
Downhill folding
Carrier Proteins
Isomerization
Stability
Subjects
Details
- Language :
- English
- ISSN :
- 00145793
- Issue :
- 3
- Database :
- OpenAIRE
- Journal :
- FEBS Letters
- Accession number :
- edsair.doi.dedup.....1b70dea2820187ce96303aabe1463f20
- Full Text :
- https://doi.org/10.1016/S0014-5793(99)00826-1