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Computational Study of the Stability of the Miniprotein Trp-Cage, the GB1 β-Hairpin, and the AK16 Peptide, under Negative Pressure
- Source :
- The Journal of Physical Chemistry B. 118:7761-7769
- Publication Year :
- 2014
- Publisher :
- American Chemical Society (ACS), 2014.
-
Abstract
- Although hot, cold, and high pressure denaturation are well characterized, the possibility of negative pressure unfolding has received much less attention. Proteins under negative pressure, however, are important in applications such as medical ultrasound, and the survival of biopoloymers in the xylem and adjacent parenchyma cells of vascular plants. In addition, negative pressure unfolding is fundamentally important in obtaining a complete understanding of protein stability and naturally complements previous studies of high pressure denaturation. We use extensive replica-exchange molecular dynamics (REMD) simulations and thermodynamic analysis to obtain folding/unfolding equilibrium phase diagrams for the miniprotein trp-cage (α-structure, 20-residue), the GB1 β-hairpin (β-structure, 16-residue), and the AK16 peptide (α-helix, 16-residue). Although the trp-cage is destabilized by negative pressure, the GB1 β-hairpin and AK16 peptide are stabilized by this condition.
- Subjects :
- chemistry.chemical_classification
Protein Conformation
Protein Stability
Chemistry
Molecular Sequence Data
Proteins
Peptide
Molecular Dynamics Simulation
Surfaces, Coatings and Films
Folding (chemistry)
Crystallography
Equilibrium phase
Molecular dynamics
High pressure
Pressure
Materials Chemistry
Biophysics
Thermodynamics
Denaturation (biochemistry)
Amino Acid Sequence
Physical and Theoretical Chemistry
Cage
Medical ultrasound
Subjects
Details
- ISSN :
- 15205207 and 15206106
- Volume :
- 118
- Database :
- OpenAIRE
- Journal :
- The Journal of Physical Chemistry B
- Accession number :
- edsair.doi.dedup.....376c1f4cbc9ab8d65f56c6eb26f45e5e