Substitution of an Internal Disulfide Bridge with a Diselenide Enhances both Foldability and Stability of Human Insulin

Keyphrases

• Insulin 100%
• Disulfide Bridge 100%
• Diselenide 100%
• Insulin Analogues 100%
• Foldability 100%
• Human Insulin 100%
• Beta Chain 66%
• Enhanced Stability 33%
• Chemical Synthesis 33%
• Selenocysteine 33%
• Cysteine Residues 33%
• Protease 33%
• 3D Structure 33%
• Insulin Resistance 33%
• 2D NMR 33%
• Gluc 33%
• X-ray Crystallography 33%
• Native-like 33%
• Lectin 33%
• Insulin Receptor 33%
• Hydrophobic Core 33%
• Guanidine 33%
• Sulfonate 33%
• Selenium 33%
• Protein Engineering 33%
• Thermodynamic Stability 33%
• Enzymatic Cleavage 33%
• Reductive Unfolding 33%
• Intra-chain 33%
• Molecular Pharmacology 33%
• Modern Treatment 33%
• Solid-phase Peptide Synthesis 33%
• Diabetes Mellitus Treatment 33%
• Steric Clash 33%
• Sulfitolysis 33%
• Denaturation Studies 33%
• Disulfide 33%
• Insulin Synthesis 33%

Chemistry

• Disulfide 100%
• Insulin Derivative 100%
• Diselenide 100%
• Insulin (Human) 100%
• stability 100%
• Selenocysteine 33%
• Two-Dimensional NMR 33%
• Denaturation 33%
• Peptide Synthesis 33%
• Selenium Atom 33%
• Lectin 33%
• Cysteine 33%
• Guanidine 33%
• Sulfonate 33%

Biochemistry, Genetics and Molecular Biology

• Disulfide 100%
• Insulin Analog 100%
• X Ray 33%
• Synthesis 33%
• Selenocysteine 33%
• Wild Type 33%
• Solid 33%
• Insulin Resistance 33%
• Peptide Synthesis 33%
• Sulfonate 33%
• Protein Engineering 33%
• Insulin Receptor 33%
• Lectin 33%
• Insulin Synthesis 33%
• Denaturation 33%
• Protease 33%
• Cysteine 33%