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. Author manuscript; available in PMC: 2013 Aug 1.
Published in final edited form as: Proteins. 2012 May 25;80(8):2046–2055. doi: 10.1002/prot.24095

TABLE II.

Comparison of secondary structure estimates from the crystal structure of residues 197-437 of mouse TIP47/perilipin-3 (Protein Data Bank entry 1SZI) with those determined from circular dichroism measurements on the full-length human TIP47/perilipin-3 and the truncation mutants

α-Helix %
(approx. no.
of residues)		 β-Strand %
(approx. no.
of residues)		 Turn %
(approx. no.
of residues)		 Random turn %
(approx. no.
of residues)
Mouse TIP47/perilipin-3197-437
crystal structure		 60 (150) 5 (13) N/D N/D
TIP47/perilipin-3187-434 40 (100) 13 (32) 20 (49) 28 (69)
TIP47/perilipin-3152-434 35 (98) 17 (48) 21 (59) 28 (79)
TIP47/perilipin-3117-434 30 (94) 18 (57) 21 (67) 31 (99)
Full-length human
TIP47/perilipin-3		 26 (113) 20 (87) 23 (100) 31 (135)