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. Author manuscript; available in PMC: 2021 Apr 26.
Published in final edited form as: Biochemistry. 2020 May 11;59(20):1871–1880. doi: 10.1021/acs.biochem.0c00159

Table 1.

Dissociation Constants for H2A.Z I and II Acetylated Peptides for 5FW-BPTF Determined by PrOF NMR Binding Experiments

Kd (μM)a
acetylation pattern H2A.Z I H2A.Z II
unacetylated   NB   NB
monoacetylated
 K4ac 1300d 1290
 K7ac 1140d  NS
 K11ac 1300d 1360
 K13ac 1810d 1730
 K15ac  NSd 1700
diacetylated
 K4ac,K7ac  990d  660
 K4ac,K11ac  780d  760
 K4ac,K13ac  780  790
 K4ac,K15ac  630  430b
 K7ac,K11ac 1200d  780
 K7ac,K13ac  520  310c
 K4me,K7ac,K13ac  ND  340
 K7ac,K15ac  750  370
 K11ac,K13ac 1440  790
 K11ac,K15ac  950  880
 K13ac,K15ac  830  910
triacetylated
 K4ac,K7ac,K11ac 1510d  810
 K7ac,K13ac,K15ac  650  960
a

NB = nonbinding. NS = nonsaturating. ND = not determined.

b

Average of two experimental replicates.

c

Average of three experimental replicates (SD ± 30 μM).

d

Affinities previously reported by Perell et al.36