. Author manuscript; available in PMC: 2009 Aug 5.

Published in final edited form as: Biochemistry. 2008 Jul 11;47(31):8094–8102. doi: 10.1021/bi800766k

Table 1.

Dissociation constants with standard deviations for selected peptides (residues 1-21) from the intensely blue pool (50 nM screen)^a, the colorless pool (2 μM screen)^b and for comparison^c as determined by ITC. Values are the averages of two or more separate assays, except for those annotated with ‘*’, in which case the error associated with the fit is reported. Dissociation constants for peptides marked with ‘x’ are approximations with relatively large errors associated with these low-affinity interactions

Peptide	PTM Position							K_d (μM)
Peptide	1	3	5	8	12	16	20	K_d (μM)
1^a	S	U	Kac	K	K	K	Kme3	2.1 ± 0.2
2^a*	Sph	R	Kac	K	K	K	Kme3	1.4 ± 0.1
3^a	S	MeR	Kac	K	Kac	Kac	Kme2	7.5 ± 1.1
*4^a^x**	S	MeR	K	Kac	Kac	K	K	190 ± 32
5^b*	Sph	Rme2s	Kac	Kac	Kac	Kac	Kme1	74.4 ± 31.5
6^bx	Sph	Rme2s	Kac	Kac	Kac	K	K	>500
7^b	Sph	U	K	Kac	Kac	Kac	K	N.D.
8^c	S	Rme2s	K	K	K	K	Kme2	3.8 ± 0.4
9^a	Sph	Rme2s	K	K	K	K	Kme2	5.8 ± 1.5
10^c	S	Rme2s	K	Kac	Kac	K	Kme2	6.7 ± 0.1
11^c	S	Rme2s	Kac	K	K	Kac	Kme2	8.8 ± 0.8
12^c	S	Rme2s	Kac	Kac	Kac	Kac	Kme2	11.6 ± 1.4
13^b	Sph	Rme2s	Kac	Kac	Kac	Kac	Kme2	25.2 ± 3.1