A native disulfide stabilizes non-native helical structures in partially folded states of equine β-lactoglobulin

Biochemistry

Volumn 50, Issue 49, 2011, Pages 10590-10597

  Yamamoto, Mio ^a   Nakagawa, Kanako ^a   Fujiwara, Kazuo ^a   Shimizu, Akio ^a   Ikeguchi, Mitsunori ^b   Ikeguchi, Masamichi ^a  

^a SOKA UNIVERSITY   (Japan)

^b YOKOHAMA CITY UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

CD SPECTRA; DISULFIDE BONDS; FOLDED STATE; HELICAL STRUCTURES; HELIX FORMATION; LACTOGLOBULIN; NON-NATIVE; REFOLDING; SITE DIRECTED MUTAGENESIS; TEAR LIPOCALIN;

COVALENT BONDS; DICHROISM;

NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY;

BETA LACTOGLOBULIN; CORE OF A HELICAL INTERMEDIATE OF BETA LACTOGLOBULIN; DISULFIDE; PEPTIDE FRAGMENT; UNCLASSIFIED DRUG;

ALPHA HELIX; ARTICLE; CIRCULAR DICHROISM; DISULFIDE BOND; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN REFOLDING; PROTEIN STRUCTURE;

AMINO ACID SUBSTITUTION; ANIMALS; CIRCULAR DICHROISM; DISULFIDES; HORSES; LACTOGLOBULINS; MAGNETIC RESONANCE SPECTROSCOPY; PEPTIDE FRAGMENTS; PROLINE; PROTEIN FOLDING;

EID: 82955194526     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi2013239     Document Type: Article

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