Title : Structural properties of high density lipoprotein subclasses homogeneous in protein composition and size.

Pub. Date : 1993 Mar 5

PMID : 8444856






1 Functional Relationships(s)
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Protein Name
Organism
1 The spectroscopic analyses indicated that the secondary structures and three-dimensional arrangements of apoA-I in all these particles are remarkably similar: their tryptophan residues are located in similar nonpolar environments and become exposed to increasing concentrations of guanidine hydrochloride in comparable denaturation steps; the 60-65% alpha-helical structures in apoA-I are denatured in similar patterns with 0-5 M denaturant concentrations. Tryptophan apolipoprotein A1 Homo sapiens