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. Author manuscript; available in PMC: 2019 Nov 1.
Published in final edited form as: J Struct Biol. 2018 Jul 30;204(2):151–164. doi: 10.1016/j.jsb.2018.07.017

Table 2.

Molecular weights and α-helical contents of PAMAp53 and its derivative truncated peptides

Protein α-helical contenta Mol. Wt. calcd. (MALDI-TOF)b Mol. Wt. AUCc
PAMAP53_short 39 % 16,845 (16,917) 28,000 rpm 15,200 ± 1,000 32,000 rpm 14,800 ± 2,000 36,000 rpm 14,400 ± 2,300
PAMAP53_medium 32 % 20,498 (20,348) 24,000 rpm 22,700 ± 500 28,000 rpm 21,500 ± 600 32.0 rpm 18.0 ± 200
PAMAP53_long 49 % 35,232 (34,937) 18,000 rpm 67,600 ± 2,500 21,000 rpm 67,600 ± 3,800 24,000 rpm 67,500 ± 4,500
PAMAP53 27 % 40,941 (41,083) 81,507d
VEK75ap53 9,119 (9136) 40,000 rpm 9,700 ± 300 46,000 8,800 ± 100
AGL55NS88.2 6,726 (6,733) 40,000 rpm 6,400 ± 200 46,000 rpm 6,700 ± 100
KTI55SS1448 6,784 (6,791) 40,000 6,900 ±120 46,000 6,400 ± 100
a

CD spectroscopy was conducted at 25° C, and α-helical content was calculated for each protein employing the mean residue ellipticities at 222 nm.

b

Calculated molecular mass from the protein linear sequence calculated by ExPASy and the (experimentally determined molecular masses from MALDI-TOF).

c

Molecular weight (Mol. Wt.) of the proteins in solution from AUC at 25° C. In all cases, single molecular weight species was observed throughout the concentration gradient in the cell. Data from the top, top, and top channels were collected and are presented as the mean ± S.D.