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Volumn 14, Issue 28, 2016, Pages 6780-6785
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Replacing a single atom accelerates the folding of a protein and increases its thermostability
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Author keywords
[No Author keywords available]
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Indexed keywords
CATALYST ACTIVITY;
CHAINS;
FLUORINE;
STABILITY;
NATIVE STRUCTURES;
PEPTIDE BONDS;
POLYPEPTIDE CHAIN;
PROLINE RESIDUES;
RIBONUCLEASE A;
SEMISYNTHESIS;
STEREOELECTRONIC EFFECT;
THREE-DIMENSIONAL STRUCTURE;
PROTEINS;
PANCREATIC RIBONUCLEASE;
PROLINE;
AMINO ACID SUBSTITUTION;
ANALOGS AND DERIVATIVES;
CHEMISTRY;
GENETICS;
HALOGENATION;
MOLECULAR MODEL;
PROTEIN CONFORMATION;
PROTEIN FOLDING;
PROTEIN STABILITY;
TEMPERATURE;
THERMODYNAMICS;
AMINO ACID SUBSTITUTION;
HALOGENATION;
MODELS, MOLECULAR;
PROLINE;
PROTEIN CONFORMATION;
PROTEIN FOLDING;
PROTEIN STABILITY;
RIBONUCLEASE, PANCREATIC;
TEMPERATURE;
THERMODYNAMICS;
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EID: 84978859462
PISSN: 14770520
EISSN: None
Source Type: Journal
DOI: 10.1039/c6ob00980h Document Type: Article |
Times cited : (21)
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References (62)
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