Changes in non-core regions stabilise plastocyanin from the thermophilic cyanobacterium Phormidium laminosum
Explore this paper's citation graph
Summary
Long-time-scale molecular dynamics simulations show that the thermophilic protein optimises a set of intramolecular interactions within the region that comprises the strands β5 and β6, loop L5 and the helix, which exhibits most of the differences in the primary sequence between the two proteins.
- Type
- article
- Published
- 2010-03-01
- Cited by
- 5
- References
- 63
- OpenAlex
- https://openalex.org/W19915878
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:7150303
Keywords
Navy, Combatant, Homeland security, National security, Terrorism
References
- The consistency of large concerted motions in proteins in molecular dynamics simulations.
- Thermal denaturation of spinach plastocyanin: effect of copper site oxidation state and molecular oxygen.
- Copper protein structures.
- The conformation of thermolysin.
- The Dielectric Constant of Water and Debye‐Hückel Limiting Law Slopes
- Copper stabilizes azurin by decreasing the unfolding rate.
- Solid model compounds and the thermodynamics of protein unfolding.
- The crystal structure of citrate synthase from the hyperthermophilic archaeon pyrococcus furiosus at 1.9 A resolution,.
- A well-behaved electrostatic potential-based method using charge restraints for deriving atomic char
- Comparison of simple potential functions for simulating liquid water
- Electrostatic contributions to the stability of hyperthermophilic proteins.
- The engineering of a more thermally stable lactate dehydrogenase by reduction of the area of a water-accessible hydrophobic surface.
- Structure-dependent relationships between growth temperature of prokaryotes and the amino acid frequency in their proteins
- The stability of proteins in extreme environments.
- Thermal unfolding of plastocyanin from the mesophilic cyanobacterium Synechocystis sp. PCC 6803 and comparison with its thermophilic counterpart from Phormidium laminosum.
- Enhanced protein thermostability from designed mutations that interact with α-helix dipoles
- Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding.
- Effects of metal ligation and oxygen on the reversibility of the thermal denaturation of Pseudomonas aeruginosa azurin.
- Contribution of electrostatic interactions, compactness and quaternary structure to protein thermostability: lessons from structural genomics of Thermotoga maritima.
- Genomic Correlates of Hyperthermostability, an Update*
Cited by
- How the local geometry of the Cu-binding site determines the thermal stability of blue copper proteins.
- Dynamics and unfolding pathway of chimeric azurin variants: insights from molecular dynamics simulation
- Modulation of copper site properties by remote residues determines the stability of plastocyanins
- Theoretical study on behavior of water molecules around spinach plastocyanin.
- Key Role of the Local Hydrophobicity in the East Patch of Plastocyanins on Their Thermal Stability and Redox Properties
Related papers
- Don't Forget About Dedicated Sea Mine Countermeasures
- The Use of Air Power for Maritime Homeland Defense
- Defense of America's Sealift
- Homeland Security is More than Homeland Defense
- Maritime Critical Infrastructure Protection: Multi-Agency Command and Control in an Asymmetric Environment
- Redefining the Littorals
- Naval Force Protection in the Littorals.
- Programs Vs. Resources: Some Options for the Navy
- Seamless Maritime Concept
- To Find, and Not to Yield: How Advances in Information and Firepower Can Transform Theater Warfare