Chemical methods for producing disulfide bonds in peptides and proteins to study folding regulation

Current Protocols in Protein Science

Volumn , Issue SUPPL.76, 2014, Pages

  Okumura, Masaki ^a   Shimamoto, Shigeru ^b   Hidaka, Yuji ^b  

^a TOHOKU UNIVERSITY   (Japan)

^b KINKI UNIVERSITY   (Japan)

Author keywords

Additive; Disulfide; Folding; Glutathione; Protein disulfide isomerase

Indexed keywords

2 DIISOPROPYLAMINOETHANETHIOL; DISULFIDE; GLUTATHIONE; GLUTATHIONE DERIVATIVE; GUANIDINE; ORGANIC SOLVENT; PROTEIN DISULFIDE ISOMERASE; REAGENT; SELENOGLUTATHIONE; SODIUM CHLORIDE; TRIFLUOROETHANOL; UNCLASSIFIED DRUG; UREA; PEPTIDE; PROTEIN; ALPHA LACTALBUMIN; ENDOTHELIN; RIBONUCLEASE A; RINDOPEPIMUT;

ARTICLE; CATALYST; CHEMICAL REACTION KINETICS; CLINICAL PROTOCOL; CONCENTRATION (PARAMETERS); CONTROLLED STUDY; DISULFIDE BOND; FRACTIONATION; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN UNFOLDING; REGULATORY MECHANISM; THERMODYNAMICS; CHEMISTRY; ALPHA HELIX; ENDOPLASMIC RETICULUM; ENZYME ACTIVE SITE; ENZYME CONFORMATION; HYDROGEN BOND; HYDROPHOBICITY; ISOMERIZATION; OXIDATION REDUCTION POTENTIAL; PRECIPITATION; PROTEIN CONFORMATION; PROTEIN CROSS LINKING; PROTEIN REFOLDING;

DISULFIDES; PEPTIDES; PROTEIN DISULFIDE-ISOMERASES; PROTEIN UNFOLDING; PROTEINS;

EID: 84906670959     PISSN: 19343655     EISSN: 19343663     Source Type: Journal    
DOI: 10.1002/0471140864.ps2807s76     Document Type: Article

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