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Literature summary for 3.1.31.1 extracted from

  • Patel, S.; Sasidhar, Y.U.
    A shorter peptide model from staphylococcal nuclease for the folding-unfolding equilibrium of a beta-hairpin shows that unfolded state has significant contribution from compact conformational states (2008), J. Struct. Biol., 164, 60-74.
    View publication on PubMed

Application

Application Comment Organism
analysis peptide model LMYKGQPM from staphylococcal nuclease can serve as model for faster folding beta-hairpins pursuing fast folding events Staphylococcus sp.

Crystallization (Commentary)

Crystallization (Comment) Organism
LMYKGQPM, short peptide model from staphylococcal nuclease to model the conformational equilibrium between a hairpin conformation and its unfolded state (molecular dynamics simulation), in water, cubic model system, total simulation time 600 ns, starting from a polyproline II conformation, GROMOS96 force field under NVT conditions, 27°C: native and non-native hairpins are very close in free energies, interconversion can happen only through the unfolded conformation. Both folding and unfolding events display single exponential kinetics Staphylococcus sp.

General Stability

General Stability Organism
native hairpin conformation is more stable than non-native conformation Staphylococcus sp.

Organism

Organism UniProt Comment Textmining
Staphylococcus sp.
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-
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Synonyms

Synonyms Comment Organism
staphylococcal nuclease
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Staphylococcus sp.