Table 1 Comparison of properties of different AHs

From: A giant amphipathic helix from a perilipin that is adapted for coating lipid droplets

AH

Positiona

Lengthb

Hydr. momc

Fract of residuesd

Lipid-binding properties

Ref

Hdr

LH

Ch

Hel 13-5

n.a.e

18

0.69

0.72

0.06

0.28

Tubulates liposomes

73

GMAP210

1–38 (1979)

38

0.48

0.37

0.05

0.05

Golgi vesicles/abundant packing defects

14, 25

Nup133

247–267 (1156)

21

0.44

0.38

0.05

0.10

Nuclear pore membrane

67

CIDEA

163–180 (219)

18

0.53

0.5

0.11

0.17

LDsf

28

CCTα

236–294 (368)

59

0.48*

0.32

0.10

0.49

Nuclear envelope/ER and LDs/liposomes

6, 16 , 64

Apolipoprotein-AI

74–267 (267)

186 (7 P)g

0.39*

0.40

0.065

0.35

Lipoprotein particles

48

α-Synuclein

1–89 (144)

89

0.30*

0.47

0.02

0.24

Synaptic vesicles/neg. charged small liposomes

44

Plin3

114–204 (434)

90

0.35*

0.37

0.01

0.23

LDs and cytosol

11

Plin4

70–1037 (1357)

968

(0.257)*

0.35

0.002

0.15

This study

 
  1. a Numbers give the first and last amino acid in the protein sequence, with the total length of each protein given in brackets
  2. b Length is based on structural data, when available, and visual inspection using Heliquest71. Prolines are considered as helix breakers
  3. c Hydrophobic moment is calculated using Heliquest74. The AHs that contain 11-mer repeats are plotted as 3–11 helices. For longer AHs (*), the mean of hydrophobic moments of consecutive helices is given (see Supplementary Fig. 1 for details)
  4. d Fraction of different amino acids in the AH sequence: Hdr, all hydrophobic (A, I, L, M, V, F, W, Y); LH, large hydrophobic (aromatic) (F, W, Y); Ch, charged=acidic (D, E) and basic (K, R)
  5. e This is an artificial AH
  6. f This AH has only been tested as a fusion with other parts of the protein, therefore its specificity for LDs is not known
  7. g The helix is broken by seven prolines, which induce a kink; ten separate helices in the structure (Supplementary Fig. 1)
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