Table 2. Percent composition of WT CPT-I bound to ACBP, L-FABP, and SCP-2 secondary structures determined by CD.

The relative proportions of the different types of secondary structures for the wild type CPTI peptide were calculated as described in “Materials and Methods”. These structures were as follows: H(r) represents regular α-helices, H(d) represents distorted α-helices, S(r) represents regular β-sheets, S(d) represents distorted β-sheets, Turns represent β-turns, and Unrd represents unordered structures.

CoA BP	Spectra	Hr (%)	Hd (%)	Sr (%)	Sd (%)	Turns (%)	Unrd (%)
ACBP	Act	13.2±0.6***	13.1±0.1***	13.8±0.4***	9.5±0.1***	22.0±0.2	28.2±0.5**
	Theor	22.0±0.4	17.1±0.3	6.3±0.6	6.7±0.2	22.6±0.4	25.4±0.8
L-FABP	Act	7.5±0.5***	9.1±0.4**	19.6±0.7***	12.2±0.2***	24.2±0.2**	28.1±0.5
	Theor	14±1	11.7±0.7	16.1±0.2	10.7±0.3	22.1±0.6	26±1
SCP-2	Act	2.7±0.4***	5.5±0.3***	20.9±0.3	12.1±0.1**	24.2±0.5*	34.4±0.9***
	Theor	6.1±0.4	8.7±0.7	21.5±0.8	11.5±0.1	22.2±0.5	27.8±0.5
CytoC	Act	43±3	24±3	4±2	5±3	13.7±0.8	14±2
	Theor	46±2	25±4	4.4±0.7	5±1	11.4±0.7	11±4

Asterisks represent significant differences between experimentally acquired data (Act) versus the theoretical average of the proteins assuming no conformational change (Theor) with * P<0.05, ** P<0.001, *** P<0.0001.