Random coil conformation of a Gly/Ala-rich insert in IκBα excludes structural stabilization as the mechanism for protection against proteasomal degradation

FEBS Letters

Volumn 440, Issue 3, 1998, Pages 365-369

  Leonchiks, Ainars ^b,c   Liepinsh, Edvards ^a   Barishev, Mikhail ^c   Sharipo, Anatoly ^b,c   Masucci, Maria G ^b   Otting, Gottfried ^a  

^a KAROLINSKA INSTITUTE   (Sweden)

^b KAROLINSKA INSTITUTE   (Sweden)

^c August Kirchenstein Institute of Microbiology and Virology   (Latvia)

Author keywords

Amino acid analysis; Gly Ala rich peptide; I B ; Nuclear magnetic resonance; Random coil conformation

Indexed keywords

ALANINE; GLYCINE; PROTEASOME;

AMINO ACID SEQUENCE; ARTICLE; CIRCULAR DICHROISM; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DEGRADATION; PROTEIN STABILITY;

ALANINE; AMINO ACID SEQUENCE; AMINO ACIDS; CYSTEINE ENDOPEPTIDASES; DNA-BINDING PROTEINS; GLYCINE; I-KAPPA B PROTEINS; MAGNETIC RESONANCE SPECTROSCOPY; MOLECULAR SEQUENCE DATA; MULTIENZYME COMPLEXES; PEPTIDES; PLIABILITY; PROTEASOME ENDOPEPTIDASE COMPLEX; PROTEIN CONFORMATION;

EID: 0032437713     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0014-5793(98)01488-4     Document Type: Article

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