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Volumn 12, Issue 5, 2006, Pages 1436-1447

A designed well-folded monomeric four-helix bundle protein prepared by Fmoc solid-phase peptide synthesis and native chemical ligation

(1) Dolphin, Gunnar T a

a UNIVERSITÉ JOSEPH FOURIER (France)

Author keywords

Helical structures; Native chemical ligation; Peptides; Protein design; Protein folding

Indexed keywords

AMINO ACIDS; HYDROPHOBICITY; MONOMERS; NUCLEAR MAGNETIC RESONANCE; PROTEINS; THERMOANALYSIS;

HELICAL STRUCTURES; NATIVE CHEMICAL LIGATION; PEPTIDES; PROTEIN DESIGN; PROTEIN FOLDING; TRIFLUOROACETIC ACID (TFA);

SYNTHESIS (CHEMICAL);

GUANIDINE; HELIX LOOP HELIX PROTEIN; PEPTIDE;

ARTICLE; CHEMISTRY; DIMERIZATION; HEAT; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; SYNTHESIS; THERMODYNAMICS; ULTRACENTRIFUGATION;

DIMERIZATION; GUANIDINE; HEAT; HELIX-LOOP-HELIX MOTIFS; PEPTIDES; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; THERMODYNAMICS; ULTRACENTRIFUGATION;

EID: 32044470021 PISSN: 09476539 EISSN: 15213765 Source Type: Journal
DOI: 10.1002/chem.200500458 Document Type: Article

Times cited : (5)

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