Packing interactions in the apomyglobin folding intermediate.

doi:10.1038/nsb0596-439

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Article

Packing interactions in the apomyglobin folding intermediate.

Nature structural biology - 1 May 1996

Kay M S, Baldwin R L

Abstract excerpt

The contribution of specific packing to the stability of the sperm whale apomyoglobin intermediate has been studied by urea denaturation monitored by circular dichroism and fluorescence. Mutations disrupting native packing sites within the subdomain formed by the A, G and H helices destabilize th...

Topics

Acids
Apoproteins
Circular Dichroism
Computer Simulation
Models, Chemical
Mutation
Myoglobin
Protein Conformation
Protein Folding
Protein Structure, Secondary
Spectrometry, Fluorescence
Urea

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