Probing the urea dependence of residual structure in denatured human α-lactalbumin

Journal of Biomolecular NMR

Volumn 45, Issue 1-2, 2009, Pages 121-131

  Higman, Victoria A ^a,c   Rösner, Heike I ^b,d   Ugolini, Raffaella ^a   Greene, Lesley H ^a,e   Redfield, Christina ^b   Smith, Lorna J ^a  

^a UNIVERSITY OF OXFORD   (United Kingdom)

^b UNIVERSITY OF OXFORD   (United Kingdom)

^c LEIBNIZ INSTITUT FÜR MOLEKULARE PHARMAKOLOGIE   (Germany)

^d UNIVERSITY OF COPENHAGEN   (Denmark)

^e OLD DOMINION UNIVERSITY   (United States)

Author keywords

15N relaxation; Denatured state; Human lactalbumin; Protein folding; Reduced spectral density mapping; Residual dipolar couplings

Indexed keywords

ALANINE; ALPHA LACTALBUMIN; CYSTEINE; NITROGEN 15; PROTON; UREA;

AMINO ACID COMPOSITION; ARTICLE; CIRCULAR DICHROISM; CONCENTRATION (PARAMETERS); CONTROLLED STUDY; HETERONUCLEAR SINGLE QUANTUM COHERENCE; HUMAN; HYDROPHOBICITY; NUCLEAR OVERHAUSER EFFECT; PH; PREDICTION; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE; STATISTICAL MODEL;

ALANINE; HUMANS; HYDROPHOBICITY; LACTALBUMIN; MODELS, MOLECULAR; NITROGEN ISOTOPES; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN DENATURATION; PROTEIN FOLDING; UREA;

EID: 69249205445     PISSN: 09252738     EISSN: 15735001     Source Type: Journal    
DOI: 10.1007/s10858-009-9342-y     Document Type: Article

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