Conserved Folding Pathways of α-Lactalbumin and Lysozyme Revealed by Kinetic CD, Fluorescence, NMR, and Interrupted Refolding Experiments

Journal of Molecular Biology

Volumn 378, Issue 3, 2008, Pages 686-698

  Schlepckow, Kai ^a   Wirmer, Julia ^a   Bachmann, Annett ^b   Kiefhaber, Thomas ^b   Schwalbe, Harald ^a  

^a GOETHE UNIVERSITY   (Germany)

^b TECHNICAL UNIVERSITY OF MUNICH   (Germany)

Author keywords

caged compounds; conserved folding pathways; lysozyme; time resolved NMR spectroscopy; lactalbumin

Indexed keywords

ALPHA LACTALBUMIN; CALCIUM ION; LYSOZYME; TRYPTOPHAN; UREA;

ARTICLE; CIRCULAR DICHROISM; EGG; FLUORESCENCE MICROSCOPY; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION;

BOVINAE;

EID: 42249096940     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2008.02.033     Document Type: Article

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