ライフサイエンスコーパス: transmembrane helices

1 is an important factor in the association of transmembrane helices.

2 t accompanied by concerted rearrangements of transmembrane helices.

3 s) sandwiched between each alphabeta pair of transmembrane helices.

4 nsert between the second and third predicted transmembrane helices.

5 erted-topology repeats, each comprising five transmembrane helices.

6 urn, may coordinate the rearrangement of the transmembrane helices.

7 dissociation of, the integrin alpha and beta transmembrane helices.

8 issue for lysines and arginines in designed transmembrane helices.

9 rst (Leu22-Lys30) and fourth (Phe131-Thr137) transmembrane helices.

10 lic cavity surrounded by 12 mostly irregular transmembrane helices.

11 ive site but causes only minor shifts in the transmembrane helices.

12 a channel formed by a twisted bundle of six transmembrane helices.

13 rnal milieu by means of gaps between splayed transmembrane helices.

14 rising one nucleotide-binding domain and six transmembrane helices.

15 vation through N-terminal association of the transmembrane helices.

16 membrane proteins below 60 kDa with up to 8 transmembrane helices.

17 rich loop that connects the fourth and fifth transmembrane helices.

18 PCPs) anchored in the inner membrane by two transmembrane helices.

19 ends or breaks that are remarkably common in transmembrane helices.

20 d by single-residue changes that destabilize transmembrane helices.

21 pore by way of an iris-like expansion of the transmembrane helices.

22 etermined to be 15.8 kDa with four predicted transmembrane helices.

23 pied a space between the slide helix and two transmembrane helices.

24 oL, NuoM, NuoN, NuoA, NuoJ and NuoK, with 55 transmembrane helices.

25 oteins up to 105 kDa and those with up to 11 transmembrane helices.

26 The structure contains six transmembrane helices.

27 ositioned at the centre, surrounded by other transmembrane helices.

28 ains two inverted structural repeats of five transmembrane helices.

29 ndoplasmic reticulum (ER) protein with eight transmembrane helices.

30 of spin labels and their proximity in three transmembrane helices.

31 etic environment of more residues within the transmembrane helices.

32 empirical data, predicted a protein with 10 transmembrane helices.

33 coordinated movement of the tightly bundled transmembrane helices.

34 his means that TH5-TH9 may form a cluster of transmembrane helices.

35 n, and a voltage sensor, formed by its S0-S4 transmembrane helices.

36 own-regulation of radioligand binding to the transmembrane helices.

37 s of the individual complexes, including 132 transmembrane helices.

38 wn to involve tilting and bending of various transmembrane helices.

39 raction networks as well as the movements of transmembrane helices.

40 f a large interior chamber that is formed by transmembrane helices.

41 ," located at the extracellular interface of transmembrane helices.

42 between the extensions to the 10th and 12th transmembrane helices.

43 s of the transporter and even within certain transmembrane helices.

44 CrgA is predicted to have two transmembrane helices.

45 gest that membrane-exposed polar residues in transmembrane helices 1 and 2 of BR may provide the mole

46 hi-values occurs at the cytosolic termini of transmembrane helices 1 and 2, which we identify as a co

47 eling studies and 2-DOG uptake revealed that transmembrane helices 1 and 5 contain amino acid residue

48 m their unexpected inability to dimerize via transmembrane helices 1 and 5.

49 rge conformational changes in their adjacent transmembrane helices 1 and 6.

50 in related transporters, is located between transmembrane helices 1 and 8 of the FIRL-fold; here, we

51 rough a direct interaction between Na(+) and transmembrane helices 1 and 8, whereas Na(+) binding at

52 suggested that aromatic residues present in transmembrane helices 1, 2, and 7 interact to form an ex

53 l suggests that aromatic residues present in transmembrane helices 1, 2, and 7 may interact to form a

54 nformation with nortriptyline wedged between transmembrane helices 1, 3, 6 and 8, blocking the transp

55 in the central binding site, located between transmembrane helices 1, 3, 6, 8 and 10, directly blocki

56 osed between extracellular loops 4 and 6 and transmembrane helices 1, 6, 10 and 11.

57 E14 leads to extensive rotation and tilt of transmembrane helices 1-3 in conjunction with repacking

58 inside the channel and seems to be closer to transmembrane helices 1-4.

59 ol molecule wedged within a groove formed by transmembrane helices 1a, 5 and 7.

60 alyzed using principal component analysis of transmembrane helices 1b and 6a.

61 -linking experiments established the role of transmembrane helices 2 and 6 in the putative dimer inte

62 ggered by the rotation of the kink angles of transmembrane helices 2 and 7 and is mediated by large c

63 imity between two conserved amino acids from transmembrane helices 3 and 7 interacting through sulfur

64 imarily achieved by a rigid body movement of transmembrane helices 3, 4, 8, and 9 relative to the res

65 for the ATP derivatives that is bordered by transmembrane helices 3, 5, 6, and 7 in human P2Y(12,) w

66 Mutations in transmembrane helices 3-6 yielded predominantly varphi-v

67 and Sav1866 from Staphylococcus aureus, two transmembrane helices (3 and 4) in the membrane domains

68 ted at K(+) binding sites positioned between transmembrane helices 4, 5, and 6.

69 tructured cytoplasmic loop region connecting transmembrane helices 5 and 6 (CL3) and show how each pr

70 ligand binding site and shear motion of the transmembrane helices 5 and 6 against the other helices.

71 Synthetic peptides with the sequence of transmembrane helices 5 and 6 of CB1R, fused to a cell-p

72 icinity of the large lumenal loop connecting transmembrane helices 5 and 6 of CP43.

73 , located near the pore-forming loop between transmembrane helices 5 and 6, prevented glycosylation,

74 pecific high-affinity sites located near the transmembrane helices 5-7 of the receptor.

75 f transmembrane helix 2 (TM2) and the top of transmembrane helices 6 and 7 (TM6-TM7) form the core of

76 discs by monitoring the spatial positions of transmembrane helices 6 and 7 at the cytoplasmic surface

77 utward movement of the extracellular ends of transmembrane helices 6 and 7.

78 hydrophobic pore in the luminal side of the transmembrane helices 6, 8, and 9.

79 buted to the two large loops of SecY linking transmembrane helices 6-7 and 8-9.

80 n of both the nucleotide binding domains and transmembrane helices 6.

81 We also show that the large loop between transmembrane helices 7 and 8 of FtsW is important for t

82 ognized cytoplasmic site in the loop between transmembrane helices 8 and 9, which influences the elec

83 -terminal pore-forming domain comprising six transmembrane helices, a pore helix, and a selectivity f

84 toplasmic extensions to the fourth and sixth transmembrane helices; a secondary, functionally less re

85 serted, however, the greater pressure on the transmembrane helices accelerates correct packing and fi

86 Only when all the transmembrane helices adopt a counterclockwise rotation,

87 hermal motion; (iii) transient separation of transmembrane helices allowed penetration of detergent m

88 substituents fine tune the configuration of transmembrane helices alphaM1-2.

89 emical data show their respective C-terminal transmembrane helices anchor the enzymes to the outer mi

90 Here we show that the 12 transmembrane helices and 2 cytosolic nucleotide-binding

91 for SLC20A1, a transmembrane protein with 12 transmembrane helices and 7 extracellular regions, that

92 es 16 different subunits, with a total of 64 transmembrane helices and 9 iron-sulphur clusters.

93 t charged segment that are predicted to form transmembrane helices and a cytosolic loop, respectively

94 The Fo motor comprises of seven transmembrane helices and a decameric c-ring and invagin

95 nterior for cotranslational insertion of the transmembrane helices and a fluidic surface for proper a

96 N-terminal membrane-embedded domain with two transmembrane helices and a large C-terminal periplasmic

97 neless version of ArnT support a model of 13 transmembrane helices and a large C-terminal region expo

98 on of the hydrophobic interactions among the transmembrane helices and a pair of hydrophobic patches

99 ane topology and the new model predicts four transmembrane helices and a potential re-entrant loop on

100 reveals a horseshoe-shaped arrangement of 19 transmembrane helices and an extracellular domain positi

101 The structures reveal nine transmembrane helices and an extramembrane cap domain th

102 odimer, with each protomer consisting of six transmembrane helices and an N-terminal cytosolic domain

103 ge and diverse family of proteins with seven transmembrane helices and common topology and, most like

104 All models revealed 12 transmembrane helices and connecting loops and represent

105 ly 94% of the polypeptide), including all 12 transmembrane helices and connecting loops, with no ster

106 p clearly resolves regions (including E1, E2 transmembrane helices and cytoplasmic tails) that were m

107 strate preference, and the importance of its transmembrane helices and disulfide bond.

108 e beta1AR define ligand-binding sites in the transmembrane helices and effector docking sites at the

109 It contains four transmembrane helices and forms a functional dimer.

110 matching of hydrophobic regions on rhodopsin transmembrane helices and hydrophobic thickness of lipid

111 s (GPCRs) have mostly focused on the role of transmembrane helices and intracellular loop regions.

112 l uncharacterized protein with two predicted transmembrane helices and is localized at the endoplasmi

113 otting, we demonstrate that GOAT contains 11 transmembrane helices and one reentrant loop.

114 zobenzene pushes apart the outer ends of the transmembrane helices and opens the channel in a light-d

115 usly, but it also interacts with most of the transmembrane helices and periplasmic regions of SecY, w

116 formatic analysis of the protein revealed 12 transmembrane helices and predicted an isoelectric point

117 g of selected side chain residues within the transmembrane helices and revealed activation-induced ch

118 gs accurately reproduced the orientations of transmembrane helices and showed a significant degree of

119 While elements in the receptor's transmembrane helices and the C-terminal alpha5 helix of

120 appear to be coupled to the reorientation of transmembrane helices and the opening of MBP, events tha

121 hannel is regulated by interplay between the transmembrane helices and the termini.

122 vity: this pulls apart the outer ends of the transmembrane helices and thereby opens an aperture, or

123 All four proteins include transmembrane helices and together form the membrane anc

124 ach subunit of the transporter contains nine transmembrane helices and two hairpins that suggest a pl

125 Scap has eight transmembrane helices and two large luminal loops, desig

126 Each subunit of the transporter contains 12 transmembrane helices and two periplasmic loops that sug

127 s demonstrated using two proteins: CrgA (two transmembrane helices) and Rv1861 (three transmembrane h

128 smembrane helices, identify 18 supernumerary transmembrane helices, and assign and model 14 supernume

129 ransition involves no major rotations of the transmembrane helices, and is instead characterized by a

130 Subunit c typically comprises two transmembrane helices, and the c ring features an ion-bi

131 t binding domain immediately adjacent to the transmembrane helices appear to control selectivity of Q

132 rules governing direct interactions between transmembrane helices are complex and not restricted to

133 investigated whether prolines in or near the transmembrane helices are essential for BCRP function.

134 e dimers with a different arrangement of the transmembrane helices are likely to be recognized differ

135 The packing structures of transmembrane helices are traditionally attributed to pa

136 r, including membrane proteins with multiple transmembrane helices, are enriched and recovered in the

137 is a lipid-facing pocket between 2 adjacent transmembrane helices (around Asp-44), at which the drug

138 quasi-symmetrical subunits, each having ten transmembrane helices arranged from helical hairpin pair

139 with two inverted structural repeats of five transmembrane helices arranged, unusually, face-to-back.

140 ified seven residues in the first and second transmembrane helices as lipid-sensing residues.

141 tely 200 ns, accompanied by movements in the transmembrane helices associated with activation.

142 t M2 is tightly associated with the adjacent transmembrane helices at the intracellular end but is mo

143 icelles, YgaP forms a homodimer with the two transmembrane helices being the dimer interface, whereas

144 two transmembrane helices) and Rv1861 (three transmembrane helices), both from Mycobacterium tubercul

145 tibodies act by conformationally locking the transmembrane helices by means of restraining the exoloo

146 ues play essential roles in the functions of transmembrane helices by mediating and stabilizing their

147 ification of introduced cysteine residues in transmembrane helices by thiol-reactive reagents, and by

148 yl acceptors are frequently observed between transmembrane helices (Calpha-H...O=C).

149 osed, indicating that local movements of the transmembrane helices can control ion access to the pore

150 structure shows a novel fold comprising four transmembrane helices capped by a cytosolic domain, and

151 The seven-transmembrane helices, conformationally distinct from th

152 There, the conformation of transmembrane helices constituting a membrane-spanning f

153 es located in a periplasmic loop between two transmembrane helices contain conserved charged residues

154 Many transmembrane helices contain serine and/or threonine re

155 increases NTPDase3 activity, mediated by the transmembrane helices containing the conserved polar res

156 Residue-residue contacts across the transmembrane helices dictate the three-dimensional topo

157 ne and a unique topology of the predicted 12 transmembrane helices distinct from any other known MDR

158 in the crystal structure, the outer ring of transmembrane helices do not pack against the pore-formi

159 rangement of three distinct domains: a seven-transmembrane helices domain (TMD), a hinge domain (HD)

160 echnique to measure pulling forces acting on transmembrane helices during their cotranslational inser

161 d MFS fold, that is, with two domains of six transmembrane helices each which are related by twofold

162 amily fold; that is, with two domains of six transmembrane helices each, related by 2-fold pseudosymm

163 t proteins, which contain two domains of six transmembrane helices each.

164 by the ligand-ectodomain interactions to the transmembrane helices either through direct hormonal con

165 As the major component of membrane proteins, transmembrane helices embedded in anisotropic bilayer en

166 The Ste24p core structure is a ring of seven transmembrane helices enclosing a voluminous cavity cont

167 sm in the AM2 transmembrane domain; the four transmembrane helices flanking the channel lumen alone s

168 Barttin consists of two transmembrane helices followed by a long intracellular c

169 atic conformational spanning of the receptor transmembrane helices followed by an energy minimization

170 The two transmembrane helices form a left-handed packing arrange

171 The structure shows transmembrane helices forming a hydrophobic pore 4 A in

172 he slipknot loop seems to strap together the transmembrane helices forming the channel.

173 g function is mediated by the interaction of transmembrane helices from both proteins.

174 dynamics initiate activating fluctuations of transmembrane helices H5 and H6 in the Meta I-Meta II eq

175 nteractions between its beta-ionone ring and transmembrane helices H5 and H6, while deprotonation of

176 econd extracellular loop (EL2) and motion of transmembrane helices H5, H6, and H7 leading to the acti

177 The forces that define the interactions of transmembrane helices have been evaluated using a model

178 erol concentration, an increased presence of transmembrane helices I and II, but a reduced presence o

179 is a small cytosolic domain inserted between transmembrane helices I and II.

180 t contain eight iron-sulphur clusters and 60 transmembrane helices, identify 18 supernumerary transme

181 mutagenesis of aromatic residues located in transmembrane helices II, IV, and V of subunit B, near g

182 short intracellular linker-helix IIS4-S5 and transmembrane helices IIS5 and IIIS6.

183 in) binds between the linker helix IIL45 and transmembrane helices IIS5, IIS6, and IIIS6 with its dib

184 STRA6 has one intramembrane and nine transmembrane helices in an intricate dimeric assembly.

185 res similar and substantial movements of the transmembrane helices in both P2X receptors and ASICs, a

186 encephalitis virus and dengue virus revealed transmembrane helices in lipid bilayers, receptor-bindin

187 functional studies to probe the movement of transmembrane helices in NorM from Neiserria gonorrheae

188 concerted fluctuations of retinal ligand and transmembrane helices in rhodopsin.

189 rted disulfide bridges linking the M1 and M3 transmembrane helices in the alpha and gamma subunits.

190 imulations were conducted of the TRPV1 S1-S4 transmembrane helices in the presence of capsaicin place

191 The pore-forming transmembrane helices in these channels are linked by sh

192 The predicted transmembrane helices in XA23 also overlap with those of

193 The predicted transmembrane helices in XA23 also overlap with those of

194 re consisting of a tetramer composed of four transmembrane helices, in which two opposing helices are

195 ltage sensor domain (VSD) consisting of four transmembrane helices, including a highly mobile S4 heli

196 omophore and triggers concerted movements of transmembrane helices, including an outward tilting of h

197 domain inserted between the second and third transmembrane helices interacts intimately with paired E

198 be a major determinant of the association of transmembrane helices into functional membrane protein o

199 l attributes describing secondary structure, transmembrane helices, intrinsically disordered regions,

200 ffer in ligand orientation and the number of transmembrane helices involved.

201 refore, that the relative positioning of the transmembrane helices is preserved in mimics of the cell

202 instead favor C-terminal dimerization of the transmembrane helices, juxtamembrane segment dissociatio

203 isting of an inverted structural repeat of 5 transmembrane helices like the leucine transporter LeuT.

204 Four single-site mutations found in the transmembrane helices (M1-M4) cause different types of d

205 revealed that the iris-like expansion of the transmembrane helices mainly results from interchain mot

206 aggregation because of the hydrophobicity of transmembrane helices, making them difficult to study us

207 tramolecular interactions so that individual transmembrane helices manifest different properties.

208 n transfer, and the membrane arm contains 78 transmembrane helices, mostly contributed by antiporter-

209 data also implied that the substrate-binding transmembrane helices move up to 10 A in NorM-NG during

210 e conformations favoring dimerization of the transmembrane helices near their N termini, dimerization

211 in bilayers stretched to match the length of transmembrane helices observed as increase of sn-1 chain

212 All six transmembrane helices of CmTMEM175 are tightly packed wi

213 ed the IC pocket-located in-between the four transmembrane helices of each human Cx26 (hCx26) monomer

214 We hypothesize that the transmembrane helices of FtsB form a stable dimeric core

215 rved polar residues in the N- and C-terminal transmembrane helices of human nucleoside triphosphate d

216 ure of three serines on the same side of the transmembrane helices of MS-DesK, triggering a switching

217 wo glutamic residues located in the adjacent transmembrane helices of NuoK are important for the ener

218 d prolines located at loops of discontinuous transmembrane helices of NuoL, NuoM, and NuoN were shown

219 yzed mutants of acid residues located in the transmembrane helices of subunits B, D, and E of Na(+)-N

220 s of inter-spin distances suggested that the transmembrane helices of TatA subunits are arranged as a

221 antiparallel helical dimer that engages the transmembrane helices of the activated receptor.

222 wn K(+) coordination sites buried within the transmembrane helices of the enzyme.

223 is face forms intersubunit contacts with the transmembrane helices of the ion channel core (M1 and M3

224 Molecular dynamics of the S1-S4 transmembrane helices of the TRPV1 in a lipid bilayer co

225 dylcholine bilayer and with the target S1-S4 transmembrane helices of TRPV1.

226 The transmembrane helices of US28 adopt an active-state-like

227 elix on the intracellular side, and by S4-S6 transmembrane helices on the lateral sides.

228 Each monomer contains 12 transmembrane helices, one more than in the bacterial ho

229 transmembrane region containing at least 26 transmembrane helices per protomer.

230 thic helix extends outwards from the ring of transmembrane helices, permitting assembly of complexes

231 , only one porelike structure containing two transmembrane helices remained at 26 mus, and none of th

232 lic cavity surrounded by 12 mostly irregular transmembrane helices represents a common structural fea

233 The arrangement of the transmembrane helices reveals hallmarks of an active con

234 ge-gated potassium (Kv) channels consists of transmembrane helices S5 and S6, the turret, the pore he

235 or is formed by a linker-helix L45 and three transmembrane helices (S5 and two S6s); 2) IIS6 contains

236 d GlpG, it has been proposed that one of the transmembrane helices (S5) of the protease can rotate to

237 pontaneous global conformation change of the transmembrane helices, similar to the motion involved in

238 aposed to membrane-anchoring domains such as transmembrane helices, sites of irreversible lipid modif

239 e protein that are allosterically coupled to transmembrane helices so as to expose ion binding sites

240 on process specific interactions between the transmembrane helices start to form.

241 nal domains, each with six largely irregular transmembrane helices surrounding an aqueous cavity open

242 cal catalytic cap domain that sits atop four transmembrane helices that anchor the enzyme in the endo

243 onsisting of a Pro-rich motif flanked by two transmembrane helices that are conserved among members o

244 ootprinting reveal ordered waters within Rho transmembrane helices that are located close to highly c

245 ue substrates evolved intrinsically-unstable transmembrane helices that both become unstructured when

246 have similar structures consisting of seven transmembrane helices that contain well-conserved sequen

247 cation by thiol-specific reagents in the two transmembrane helices that form the pore (TM1 and TM2).

248 en conformation by altering the structure of transmembrane helices that line the cavity.

249 ontains a nucleotide-binding domain and four transmembrane helices that protrude in the periplasm int

250 the mutual interplay of interactions between transmembrane helices, the cytoplasmic talin protein, an

251 imers, by holding apart the N termini of the transmembrane helices, the extracellular domains instead

252 Containing 10 transmembrane helices, the two halves of NCX_Mj share a

253 c methods used to assign the topology of the transmembrane helices, these two types of structure pred

254 s intramolecular signaling chain through the transmembrane helices; this chain connects chemokine bin

255 Many transmembrane helices tilt and shift positions, and the

256 Scap has eight transmembrane helices (TM) joined by four small hydrophi

257 t Na,K-ATPase activity, whereas mutations in transmembrane helices (TM), alphaTM2 and alphaTM4, aboli

258 During the gating process, both the transmembrane helices TM1 and TM2 cooperatively rotate i

259 r, in homodimeric configurations with either transmembrane helices TM1/H8 or TM4/3 at the interface,

260 ane topology with an intracellular loop, two transmembrane helices (TM1 and TM2), and extracellular N

261 te homotrimers, with each subunit having two transmembrane helices, TM1 and TM2.

262 Here, we propose nine residues in transmembrane helices (TM2, TM3, and TM5) that potential

263 d interactions between the cytosolic ends of transmembrane helices TM3 and TM6 of class-A (rhodopsin-

264 en the helix HP1b on the hairpin HP1 and the transmembrane helices TM7 and TM8, using the high resolu

265 o three prolines located in the odd-numbered transmembrane helices (TMH), Pro-27, Pro-132, and Pro-22

266 xperiments with synthetic peptides mimicking transmembrane helices (TMH), we show that such superpote

267 The CbuD1884 protein contains two transmembrane helices (TMHs) and a coiled-coil domain pr

268 Ag(+)(Cd(+2))-sensitive Cys extends from the transmembrane helices (TMHs) of subunits a and c into cy

269 in (Cdr1p) that correspond to each of the 12 transmembrane helices (TMHs) of the two transmembrane do

270 ting of an N-terminal domain containing four transmembrane helices (TMHs), a large central periplasmi

271 lerae, reveals a protein fold composed of 12 transmembrane helices (TMHs), confirming hydropathy anal

272 rotations about the axis (eta) of all seven transmembrane helices (TMHs), showing that the experimen

273 ed in the transport mechanism, in particular transmembrane helices (TMs) 1a and 7 as well as extracel

274 ns (NBDs) with conformational changes in its transmembrane helices (TMs) is poorly defined.

275 cording to this model, sialin consists of 12 transmembrane helices (TMs) with an overall architecture

276 ucture of NhaA, solved at pH 4, comprises 12 transmembrane helices (TMs), arranged in two domains, wi

277 30-residue TEB4-Doa10 domain, includes three transmembrane helices (TMs).

278 (secondary structure, solvent accessibility, transmembrane helices (TMSEG) and strands, coiled-coil r

279 cellular ligand binding events through their transmembrane helices to activate intracellular G protei

280 We propose that this transition enables the transmembrane helices to adopt a distinct conformation t

281 utilize the expanded model encompassing six transmembrane helices to calculate the RyR1 pore region

282 l constraint is released that allows the two transmembrane helices to come together to facilitate act

283 embrane (the turret) and that joins with the transmembrane helices to form the ion permeation pathway

284 ake advantage of hydrophobic interactions of transmembrane helices to manipulate the assembly of ssMP

285 iston-like or rotational displacement of the transmembrane helices to modulate activity of the linked

286 The transmembrane helices undergo relative movement to creat

287 ered potential rearrangement of at least two transmembrane helices upon Na(+)-induced drug export.

288 ocket was narrowed down to the upper part of transmembrane helices V, VI, VII and the extracellular l

289 large-scale structural rearrangements of the transmembrane helices via dynamic hydrogen bond and salt

290 MCU has two predicted transmembrane helices, which are separated by a highly c

291 switch between alternative crossings of the transmembrane helices, which form dimeric structures.

292 a closely packed bundle of mutually aligned transmembrane helices, which is further stabilized by a

293 quires an N-terminal interaction between the transmembrane helices, which promotes an antiparallel in

294 se transporter FucP and have identified four transmembrane helices whose ends close to form a predict

295 tached to lipid bilayers through hydrophobic transmembrane helices, whose topogenesis requires sophis

296 and AdipoR2 were predicted to contain seven transmembrane helices with the opposite topology to G-pr

297 e of rhomboid proteases reveal a core of six transmembrane helices, with the active-site residues res

298 The structure contains 12 transmembrane helices, with the first 10 consisting of a

299 AREpins simultaneously zippering their SNARE transmembrane helices within the freshly fused bilayers

300 edge of the topological organization of Hhat transmembrane helices would enhance our understanding of