Pages that link to "Item:Q2186542"
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The following pages link to Cooperativity of the oxidization of cysteines in globular proteins (Q2186542):
Displaying 8 items.
- In silico identification of the protein disulfide isomerase family from a protozoan parasite (Q936047) (← links)
- Predicting the disulfide bonding state of cysteines with combinations of kernel machines (Q1430038) (← links)
- pSSbond-PseAAC: prediction of disulfide bonding sites by integration of PseAAC and statistical moments (Q1717058) (← links)
- Predicting the state of cysteines based on sequence information (Q1733013) (← links)
- Conformational characterization of disulfide bonds: a tool for protein classification (Q1733034) (← links)
- Exploring synonymous codon usage preferences of disulfide-bonded and non-disulfide bonded cysteines in the \textit{E. coli} genome (Q2199211) (← links)
- Structural study of two proteins SigE and ORF1 to predict their roles in the biochemical oxidation of sulfur anions via the global sulfur oxidation operon (sox) (Q2500389) (← links)
- Comparative structural modeling of cysteine and selenocysteine (Q2885018) (← links)