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Volumn 8, Issue 16, 2002, Pages 3687-3697
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Control of lysine reactivity in four-helix bundle proteins by site-selective pKa depression: Expanding the versatility of proteins by postsynthetic functionalisation
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Author keywords
De novo design; Helical structures; Lysine reactivity; Peptides; Site selective functionalisation
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Indexed keywords
ACYLATION;
DIMERIZATION;
DIMERS;
HIGH PERFORMANCE LIQUID CHROMATOGRAPHY;
HYDROPHOBICITY;
MASS SPECTROMETRY;
NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY;
PH EFFECTS;
REACTIVITY SITES;
PROTEINS;
ALANINE;
FUMARIC ACID DERIVATIVE;
LYSINE;
ORNITHINE;
POLYPEPTIDE;
PROTEIN;
SOLVENT;
TRYPSIN;
ACYLATION;
ARTICLE;
CHEMICAL REACTION;
CIRCULAR DICHROISM;
HIGH PERFORMANCE LIQUID CHROMATOGRAPHY;
MASS SPECTROMETRY;
NUCLEAR OVERHAUSER EFFECT;
PH;
PKA;
PROTEIN FOLDING;
PROTON NUCLEAR MAGNETIC RESONANCE;
ACYLATION;
AMINO ACID SEQUENCE;
CHROMATOGRAPHY, HIGH PRESSURE LIQUID;
CIRCULAR DICHROISM;
HELIX-LOOP-HELIX MOTIFS;
HYDROGEN-ION CONCENTRATION;
HYDROPHOBICITY;
LYSINE;
MAGNETIC RESONANCE SPECTROSCOPY;
MASS SPECTROMETRY;
MODELS, MOLECULAR;
MOLECULAR SEQUENCE DATA;
PEPTIDES;
PROTEIN ENGINEERING;
PROTEIN STRUCTURE, SECONDARY;
PROTEINS;
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EID: 0037119283
PISSN: 09476539
EISSN: None
Source Type: Journal
DOI: 10.1002/1521-3765(20020816)8:16<3687::AID-CHEM3687>3.0.CO;2-8 Document Type: Article |
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Times cited : (32)
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References (33)
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