ライフサイエンスコーパス: beta-sheet

1 main fold (hydrophobic core, loop 1, loop 2, beta-sheet).

2 ell-structured intermolecular three-stranded beta sheet.

3 phipathic two- or three- strand antiparallel beta sheet.

4 s formed as the peptide augments the protein beta-sheet.

5 ge site as an extra beta-strand in a central beta-sheet.

6 atients, which indicated an overall shift to beta-sheet.

7 eous increase in the content of antiparallel-beta-sheet.

8 strands, can contain a significant amount of beta-sheet.

9 of MUC5B) were found to be dominated by the beta-sheet.

10 o insoluble amyloid fibrils that are rich in beta-sheets.

11 module) show that it assembles with parallel beta-sheets.

12 n within amelogenin that self-assembles into beta-sheets.

13 ls, whereas the oligomers form predominantly beta-sheets.

14 to the high propensity of threonine to form beta-sheets.

15 canonical beta-sandwich fold comprising two beta-sheets.

16 s and fibrillar oligomers with only parallel beta-sheets.

17 imulations with 40 A crowders result in only beta-sheets.

18 trimer subunits surrounded by three pairs of beta-sheets.

19 ther design of disulfide-tethered "turnless" beta-sheets.

20 inclusions specifically enriched in amyloid beta-sheets.

21 nd segment, 15-25 WT, forms non-toxic labile beta-sheets.

22 drophobic core, and without alpha-helices or beta-sheets.

23 cm(-1)), H-bonded parallel- and antiparallel-beta-sheets (1690cm(-1)) and H-bonded beta-turns (1664cm

24 none binding site close to helix D and E and beta-sheets 2A.

25 nding takes place at a basic patch on top of beta-sheet A and is different from other heparin-binding

26 Together, basic residues of central beta-sheet A contribute to heparin binding and activatio

27 can be formed by folding an out-of-register beta-sheet, a common type of structure found in amyloid

28 ntiparallel manner to form an intermolecular beta-sheet, affect G fusion properties.

29 synuclein (alphaS) self-assembles into toxic beta-sheet aggregates in Parkinson's disease, while it i

30 an interacting template that rapidly forces beta-sheet aggregation of C-36 to distinct amyloid speci

31 rection and head-to-tail arrangement of such beta-sheets along the c-direction.

32 ling force can facilitate the alpha-helix to beta-sheet (alpha-to-beta) transition by lowering the fr

33 entral part of the molecule representing the beta-sheet also maintained approximately 62% killing act

34 Proteins that self-assemble as cross-beta sheet amyloids are a defining pathological feature

35 ] and [URE3] are folded in-register parallel beta-sheet amyloids of Sup35p and Ure2p, respectively.

36 antibodies BVK and Synagis (Syn) using both beta-sheet and coiled-coil linkers.

37 a-helices act as a transient intermediate to beta-sheet and fibril formation of pEAbeta (3-42).

38 teractions between the highly stable central beta-sheet and flanking alpha-helices and loop regions a

39 action surface of nNOS-PDZ involves its main beta-sheet and its specific C-terminal beta-finger.

40 a-helical in the cytosol and acquires a more beta-sheet and random coil character in the nucleus.

41 important hinge-bbeta region between the PAS beta-sheet and the N-terminal cap helix that in turn des

42 structures by intermolecular hydrogen bonded beta-sheets and aggregates.

43 relaxation dynamics of the peptide backbone, beta-sheets and beta-turns, and negatively charged aspar

44 ligomers that consist of mainly antiparallel beta-sheets and fibrillar oligomers with only parallel b

45 rferon activation domain, including a set of beta-sheets and loops that serve as the binding site for

46 residues at specific positions may stabilize beta-sheets and lower the energy barrier for cross-speci

47 of Abeta can preferentially segregate within beta-sheets and that the resulting segregated beta-sheet

48 n native proteins are often formed by curved beta sheets, and the ability to control beta-sheet curva

49 allel beta-sheet, beta-turns, intermolecular beta-sheet, and aggregation of proteins.

50 s proline isomerization, reorganization of a beta-sheet, and insertion of the N-terminal alpha-helix

51 ptide amphiphiles engaged in hydrogen-bonded beta-sheets, and chromophore amphiphiles driven to assem

52 t 1.45 A revealed a novel oligomeric form of beta-sheet antimicrobial peptides within the unit cell:

53 elineate the structure and function of these beta-sheet antimicrobial peptides.

54 amyloid fibrils with a parallel in-register beta-sheet architecture and beta-sheet core mapping to r

55 structure between antiparallel and parallel beta-sheet architectures.

56 rate that structured elements, most notably, beta-sheets, are significantly concentrated in the highl

57 analysis of the dipeptide 1 showed parallel beta-sheet arrangement along the b-direction and head-to

58 crystallography reveals that the macrocyclic beta-sheet assembles to form double-walled nanotubes, wi

59 ctroscopic probe with which to elucidate the beta-sheet assembly and interaction: (1)H,(15)N HSQC stu

60 ganic solvents and water via hydrogen-bonded beta-sheet assembly as evidenced from IR spectroscopy an

61 o provide non-covalent cross-linking through beta-sheet assembly, reinforced with a polymer backbone

62 TAIL protein that folds into an antiparallel beta-sheet at the A/W interface and presents strong inte

63 Early folding of the predominantly beta-sheet ATIII domain in this two-domain protein const

64 hape of the nanostructures or their internal beta-sheet backbone, but must involve accessible adaptiv

65 coil, with the structured alpha-helices and beta-sheets being confined to the genomically defined st

66 ctures lead to the formation of antiparallel beta-sheet, beta-turns, intermolecular beta-sheet, and a

67 ps and provide evidence that the more global beta-sheet/beta-sheet facial complementarity is a critic

68 ixes alpha3 and alpha4 interact with the Vif beta-sheet (beta2-beta5).

69 ccurs via the formation of an intermolecular beta-sheet between the membrane-proximal (third) Fibrone

70 cceptors, ammonium groups, and a hydrophilic beta-sheet breaker element provides valuable insight for

71 a novel class of conformationally restricted beta-sheet breaker hybrid peptidomimetics (BSBHps).

72 onformational transition from random coil to beta-sheet by changing the pH from acidic to alkaline.

73 sidues K38 and K51, which are present on the beta-sheet C and D, form salt bridges with the head grou

74 that NMR data strongly suggest antiparallel beta-sheet calcitonin assembly, whereas modeling studies

75 eta-sheets and that the resulting segregated beta-sheets can further coassemble.

76 but TTPA contains an additional antiparallel beta-sheet carrying a lectin-like domain that could be r

77 tial disulfide bonds that reside outside the beta-sheet catalytic core but likely assist the folding

78 A shift from alpha-helix to beta-sheet conformation of proteins indicated that conce

79 soluble Abeta can switch from helicoidal to beta-sheet conformation, promoting its assembly into oli

80 pecific polypeptide chain in a regular cross-beta-sheet conformation.

81 n the fibril are arranged in an antiparallel beta-sheet conformation.

82 pentapeptides transform from alpha-helix to beta-sheet conformation.

83 ned to adopt two- or three-stranded parallel beta-sheet conformations in aqueous solution.

84 ntaining a beta hairpin and an anti-parallel beta sheet consisting of strands from the top and bottom

85 The V3 label spectrum indicates that the beta-sheet contacts between strands I and II are well fo

86 least the 13-mer as well as partially folded beta-sheet containing oligomers are coexisting.

87 the supramolecular assembly of a macrocyclic beta-sheet containing residues 16-22 of the beta-amyloid

88 ed (-)OOC-Ca(2+) interactions and changes in beta sheet content in response to variations in protein/

89 sizes, with different extents and nature of beta-sheet content and exposed hydrophobicity, they all

90 In particular, an increased beta-sheet content corresponds to a reduction in oxygen

91 ometry and variable levels of intermolecular beta-sheet content in their protein shells.

92 ydrophobic crowders reduces the antiparallel beta-sheet content of fibrils, whereas hard sphere crowd

93 rP(120-144) aggregates contain more parallel beta-sheet content than those formed by BV- and SHaPrP(1

94 ucture motifs at longer Q-lengths, including beta-sheet content that seems to contribute to the forma

95 ed oligomers exhibit a significant amount of beta-sheet content.

96 of each oligomer generally exhibit increased beta-sheet content.

97 d at 25 degrees C for 18min exhibited higher beta-sheet contents and more chemical bonds such as hydr

98 The alpha-helix and beta-sheet contents decreased, while aggregated beta-she

99 r, these oligomers undergo an alpha-helix to beta-sheet conversion catalyzed by lipid vesicles and di

100 Its folding is complex, the beta-sheet core forms early and is present in both inter

101 llel in-register beta-sheet architecture and beta-sheet core mapping to residues approximately 112-13

102 hermore, our finding that a relatively short beta-sheet core of PrP23-144 fibrils (residues approxima

103 In contrast to the stable beta-sheet core, the peripheral alpha-helices display si

104 fibrils with extended proteinase-K resistant beta-sheet cores and infrared spectra that are more remi

105 tein's conformational dynamics by disrupting beta-sheet coupling between EF hands.

106 Also, due to the ability of the non-covalent beta-sheet cross-links to reassemble, the hydrogels can

107 th and extensibility arising from their high-beta-sheet crystal contents as natural materials.

108 ifs range from multi-beta-strand barrels, to beta-sheet cups and baskets covered by alpha-helical lid

109 , we investigated the mechanisms controlling beta-sheet curvature by studying the geometry of beta sh

110 match the computational models, showing that beta-sheet curvature can be controlled with atomic-level

111 rved beta sheets, and the ability to control beta-sheet curvature would allow design of binding prote

112 t, as temperature increased, alpha-helix and beta-sheet decreased, but aggregated beta-sheet, turns a

113 retard the formation of parallel in-register beta-sheet dimers during the nucleation stage by increas

114 al cohesive structures exist on the basis of beta-sheet discontinuous domains.

115 twisted beta-sheets with an increased inter-beta-sheet distance and a higher solvent exposure than W

116 d ionic interactions between residues in the beta-sheet domain that reduce the width of the cavity.

117 We show here that a predicted beta-sheet domain, which is conserved among alphaherpesv

118 binds to SOD1 via both its alpha-helical and beta-sheet domains at the native dimer interface that be

119 rated in regions between the alpha-helix and beta-sheet domains.

120 ing of the Amyloid-beta (Abeta) peptide into beta-sheet enriched conformations was proposed as an ear

121 These findings are supported by the beta-sheet features observed by FTIR.

122 olar excess of EAK16-II, a betaFP that forms beta-sheet fibrils at high salt concentrations.

123 wild-type Abeta into distinct anti-parallel beta-sheet fibrils.

124 ed to form a large 10-stranded, antiparallel beta-sheet flanked by alpha-helices on each side, repres

125 ow that the RBM5 OCRE domain adopts a unique beta-sheet fold.

126 ackbone aminated peptides that readily adopt beta-sheet folds.

127 Folding is initiated in the turns and the beta-sheets form last.

128 pitopes cluster on the inner strands of both beta-sheets forming the fibronectin domains.

129 A designed beta-sheet-forming l-Ala-l-Val dipeptide containing azid

130 d Cap molecules were conjugated onto a short beta-sheet-forming peptide (Sup35) to yield three differ

131 In the second phase, beta-sheet forms in the polyQ.

132 h just a six-helix bundle and a six-stranded beta-sheet, forms a genome-delivery apparatus and joins

133 s of protein misfolding and the key role the beta-sheet geometry acquired in the early stages of the

134 ation function (AF) region, encompassing the beta-sheet-H6 region of the protein.

135 The two parallel beta-sheets have swapped their last beta-strands giving

136 -sheet curvature by studying the geometry of beta sheets in naturally occurring protein structures an

137 revealed random coil structure in OD-FPH and beta-sheet in FD-FPH samples.

138 tially induces opposite motions of the major beta-sheet in this channel mutant.

139 The contents of beta-sheets in dough and disulfide groups in gluten of t

140 ng between the extruded hairpin and a distal beta-sheet, in an intermolecular chain reaction similar

141 The folds of alpha-helices and beta-sheets interacted together to form a hydrophobic ca

142 equences that show inter- or intra-molecular beta-sheet interactions significant enough to form aggre

143 models of cystatin amyloid fibrils where the beta-sheet is assumed to retain its native antiparallel

144 the dynamic association of the MTS with the beta-sheet is fine-tuned to balance MinE's need to sense

145 stable core encompassing most of the central beta-sheet is highly structured and alpha-helix 3, which

146 ss uncommon structure features such as split beta-sheets, left-handed connections, and crossing loops

147 ) at their C-terminal, self-assemble to form beta-sheet like structures upon mixing.

148 enon-like intercapsomer joints, and abundant beta-sheet-like mainchain:mainchain intermolecular inter

149 licity, while both parallel and antiparallel beta-sheet-like structures are realized.

150 that one segment, 19-29 S20G, forms pairs of beta-sheets mated by a dry interface that share structur

151 , in our parallel in-register intermolecular beta-sheet model of PrP(Sc), not only would these lysine

152 Using a standard 3-stranded beta-sheet model, the WW domain, it was found that the p

153 that two complementary pentapeptides from a beta-sheet motif of a protein, being connected to an aro

154 jority of the gel forming peptides present a beta-sheet motif that is composed of alternating hydroph

155 e amino acid interactions in an antiparallel beta-sheet motif.

156 P results in self-assembly of nonaggregating beta-sheet nanofibers with precise structure.

157 In the beta-sheet, nearly all bonds are weakly correlated, and

158 e reveals that ipilimumab contacts the front beta-sheet of CTLA-4 and intersects with the CTLA-4:Beta

159 the A32-like subregion and the seven-layered beta-sheet of the gp41-interactive region of gp120.

160 re not observed with TEM, but highly ordered beta-sheets of amyloid secondary structure is identified

161 no acid residues fall on the alpha-helix and beta-sheets of the peptide-binding domain located at the

162 random coil structure, evolves into ordered beta-sheet oligomers containing at least 5 strands, and

163 a shape that is incapable of forming ordered beta-sheets or fibrils.

164 ng from thin peptide films shows features of beta-sheet ordering for both peptides, along with eviden

165 Investigation of beta-sheet-oriented conformational transitions in silk p

166 n antiparallel beta-strands organized in two beta-sheets, packed into a beta-sandwich structure that

167 of the experimentally observed antiparallel beta-sheet packing.

168 Here we report a new class of designed beta-sheet peptide dimers with strand-central disulfides

169 By altering the beta-sheet peptide graft density and concentration, we c

170 This self-healing polymer-beta-sheet peptide hybrid hydrogel with tailorable mecha

171 ysis of the structural features of different beta-sheet peptide hydrogels and their mechanical proper

172 Conjugation of beta-sheet peptide motif to the CHP results in self-asse

173 s 11-17 of IAPP (RLANFLV) into a macrocyclic beta-sheet peptide results in a monomeric peptide that d

174 and tryptophan, and D-IK8, an eight residue beta-sheet peptide) against multidrug resistant staphylo

175 al characterization of the assembly of these beta-sheet peptides has been refined recently.

176 paper, we study the assembly of macrocyclic beta-sheet peptides that contain residues 17-23 (LVFFAED

177 unctionalization of its repeating units with beta-sheet peptides to form a hydrogel, it can easily be

178 lly cross-linked via grafted self-assembling beta-sheet peptides to provide non-covalent cross-linkin

179 d a beta-sandwich fold, with the face of one beta-sheet possessing the beta-1,3-glucan-binding surfac

180 main conformation comprised of two layers of beta-sheets possessing antiparallel beta-strands with ea

181 n frequency of amide-I, amide-II, amide-III, beta-sheet protein, alpha-tocopherol and Soybean Kunitz

182 facial hydration network are observed in the beta-sheet protein.

183 ich are prototypical examples of helical and beta-sheet proteins, respectively.

184 he protein surface of both alpha-helical and beta-sheet proteins.

185 ural form consisting of laterally associated beta-sheet protofilaments that may be adopted as an alte

186 tation of the myosin lever arm, coupled to a beta-sheet rearrangement.

187 omoted allosteric signaling from the helix 6/beta-sheet region of LRH-1 to the activation function su

188 These results reveal the importance of the beta-sheet region of lysozyme for initiating self-assemb

189 sidues (I476 and V482) were within coiled or beta-sheet regions in domain B distant to the active sit

190 bound cooperatively, but those derived from beta-sheet regions in LF did not, suggesting that an all

191 more efficiently than peptides derived from beta-sheet regions of LF.

192 alline material in which the alpha-helix and beta-sheet regions of the protein are similar to crystal

193 in that has the capacity to assemble to form beta-sheet rich fibrils.

194 beta-Sheet-rich Abeta(1-42) aggregates entered the cells

195 r data therefore imply that the formation of beta-sheet-rich aggregates is a prerequisite for Abeta(1

196 that undergo a spectral shift when bound to beta-sheet-rich aggregates.

197 ild-type medin, by contrast, aggregates into beta-sheet-rich amyloid-like fibrils within 50 h.

198 heir native-like properties and convert into beta-sheet-rich amyloid-like structures, as indicated by

199 concentrations and maintained CsgA in a non-beta-sheet-rich conformation.

200 lical cellular prion protein (PrP(C)) into a beta-sheet-rich disease-causing isoform (PrP(Sc)) is the

201 ) prion protein, from disordered monomers to beta-sheet-rich fibrillar structures.

202 Elucidating the role of these beta-sheet-rich fibrils in disease progression is crucia

203 ic Zn(2+)-dependent homophilic bonds between beta-sheet-rich G5-E domains on neighboring cells.

204 sCT.heparin complexes form beta-sheet-rich heparin-covered fibrils.

205 FXXN motif in D-Wt induces the formation of beta-sheet-rich oligomeric protofibrils, which are impor

206 y disordered, monomeric alpha-synuclein into beta-sheet-rich oligomers and fibrils is associated with

207 uce conformational changes in three distinct beta-sheet-rich oligomers of the prion protein PrP, a pr

208 The formation of insoluble beta-sheet-rich protein structures known as amyloid fibr

209 Amyloids are highly ordered, cross-beta-sheet-rich protein/peptide aggregates associated wi

210 eta (3-42) has an increased tendency to form beta-sheet-rich structures compared to Abeta (1-42), as

211 s, Mcc naturally exists as two conformers: a beta-sheet-rich, protease-resistant, aggregated, inactiv

212 The characteristic 2D IR features of amyloid beta-sheet secondary structure are created by as few as

213 We have examined whether parallel beta-sheet secondary structure becomes more stable as th

214 e elicited antibodies to the peptide and the beta-sheet secondary structure conformation.

215 with glutaraldehyde until it reached a high beta-sheet secondary structure content, and species betw

216 beta-Sheet secondary structure is a common feature of am

217 dies selected to specifically react with the beta-sheet secondary structure of pathological oligomeri

218 lzheimer's disease (AD) brain, share similar beta-sheet secondary structures, but it is not known whe

219 width of which reflects the curvature of the beta-sheet segment.

220 The beta-sheet self-assembles to form long fibrils with the

221 A new capsule based on a beta-sheet self-assembling cyclic peptide with the abili

222 ils in vitro and is a major signal for cross-beta-sheet self-association of the 49-mer Phe521Leufs pe

223 channel prefers alpha-helical sequences over beta-sheet sequences.

224 on the hierarchic pathway by which distinct beta-sheets sequentially unfold using the unique possibi

225 h revealed that this protein contained three beta-sheets, seven alpha-helices, and coils.

226 anized around a central core of antiparallel beta-sheet, showing an N-terminal alpha/beta region at o

227 protein fold of a four-stranded antiparallel beta-sheet stabilized by a crossing-over alpha-helix.

228 A taxonomy of the oligomer species based on beta-sheet stacking topologies is proposed.

229 e binding and contain a characteristic cross-beta sheet structure, as revealed by x-ray scattering.

230 This fibril core has an in-register parallel beta-sheet structure and does not include the Q-rich, pr

231 l acidic region of Ng peptide pries open the beta-sheet structure between the Ca(2+) binding loops pa

232 anged in a rigid conformation, and confirm a beta-sheet structure in an assigned stretch of three ami

233 se two regions promote aggregation and adopt beta-sheet structure in the fibrils, and may also do so

234 ll-known intermolecular in-register parallel beta-sheet structure in the mature fibrils.

235 In arrestin, a modest loss of beta-sheet structure indicates an increase in flexibilit

236 is distinct from the intermolecular parallel beta-sheet structure observed in mature fibrils.

237 e that is distinct from the type 1 trimeric, beta-sheet structure of Dut80alpha.

238 teraction of a collagen beta-strand with the beta-sheet structure of Fn modules seen in the high reso

239 thesize that NUCB1 binds to the common cross-beta-sheet structure of protofibril aggregates to "cap"

240 that the extracellular sequence of C99 forms beta-sheet structure upon interaction with membrane bila

241 e gKDelta31-68 mutation spans a well-defined beta-sheet structure within the amino terminus of gK, wh

242 As a result of their distinct beta-sheet structure, 1-108-alphaS fibrils resist incorp

243 ular hydrogen bonding, including an extended beta-sheet structure, as well as aromatic interactions.

244 ally recognizes alpha-helical structure over beta-sheet structure.

245 rmolecular beta-sheets, which form the cross-beta-sheet structure.

246 hthalene-8-sulphonic acid and lack extensive beta-sheet structure.

247 d interacts with the stalk to form a compact beta-sheet structure.

248 intermediates proceed to convert into stable beta-sheet structured species and maintain their stackin

249 The population of beta-sheet structured species is >5% within 5 min of agg

250 oppositely charged ionic segments that form beta-sheet-structured hydrogel assemblies via polyion co

251 mising attributes and unique features of the beta-sheet-structured PIC hydrogels described here highl

252 ually results in the emergence of detectable beta-sheet structures according to thioflavin-T assay.

253 seases contain antiparallel, out-of-register beta-sheet structures and identifies a target for struct

254 h very high sequence identity can form cross-beta-sheet structures of sufficient stringency for incor

255 dynamics in general are more retarded around beta-sheet structures than alpha-helical motifs.

256 on of PrP from alpha-helical structures into beta-sheet structures was confirmed by circular dichrois

257 he occurrence of new bands due to aggregated beta-sheet structures, all of which indicate protein den

258 in turn stability and formation of extended beta-sheet structures.

259 mation of extended, linear preprotofibrillar beta-sheet structures.

260 eta species and induced a rapid formation of beta-sheet structures.

261 of very slow rates of rearrangement of their beta-sheet structures.

262 ins are proteins consist of three sequential beta-sheet subdomains that bind to specific carbohydrate

263 However, the in-register parallel beta-sheet supramolecular structure, indicated by interm

264 veal the presence of beta-hairpin-containing beta-sheets that are connected through interdigitating e

265 The peptide forms amphiphilic parallel beta-sheets that assemble into stacked bilayers with alt

266 try revealed altered packing arrangements of beta-sheets that encompass residues 139 and 186 of PrP(S

267 These peptides form beta-sheets that further associate into hexamers, octame

268 rmediate with a register-shift in one of the beta-sheets that was visited along a minor folding pathw

269 ble through intermolecular hydrogen bonds to beta-sheets thereby placing the azide and alkyne motifs

270 When placed into the turn of a beta-sheet, this leads to a pH switch of folding.

271 state and into an uncommon twisted parallel beta-sheet through intermolecular H-bonding in the cryst

272 emonstrated in this article, the redesign of beta-sheets to contain a global, or local, pH-dependent

273 f subunit interface, altering the packing of beta-sheets to induce changes that lead to asynchronous

274 beta-hairpin and rearrangement of the native beta-sheet topology.

275 n, de novo, a series of proteins with curved beta sheets topped with alpha helices.

276 ctive role with respect to the generation of beta-sheet toxic structures during alphaS fibrillation.

277 exibility of the TMD in terms of alpha-helix/beta-sheet transitions in model membranes (measured by i

278 a-sheet contents decreased, while aggregated beta-sheet, turns and random coil contents increased as

279 lix and beta-sheet decreased, but aggregated beta-sheet, turns and random coil increased.

280 spectroscopy can identify the highly ordered beta-sheets typical of amyloid secondary structure even

281 d by a previously unseen conformation of the beta-sheet underlying the nucleotide pocket.

282 xplored the effect of bending aromatic amide beta-sheets using building blocks that impart curvature.

283 al segments flanking a central bent aromatic beta-sheet were then synthesized and shown to form well-

284 condary structure (increase in the amount of beta-sheets) were observed while the tertiary structure

285 rdered monomers to alpha-helices and then to beta-sheets when the proteins encounter the cell membran

286 are highly stable when assembled in parallel beta-sheets, whereas they quickly unfold in antiparallel

287 f positively selected sites at the helix and beta-sheets, which are less tolerant to molecular adapta

288 many stranded and repetitive intermolecular beta-sheets, which form the cross-beta-sheet structure.

289 mic transition from the alpha-helices to the beta-sheets, which marks the onset of plastic deformatio

290 quence in the major groove while inserting a beta sheet 'wing' into the adjacent minor groove.

291 f rhodopsin forms an extended intermolecular beta sheet with the N-terminal beta strands of arrestin.

292 s and a layer of three-stranded antiparallel beta-sheet with flexible N and C termini.

293 ex is composed of a continuous nine-stranded beta-sheet with four strands from IntS9 and five from In

294 hitecture which consists of two antiparallel beta-sheets with 7 main strands, packing against each ot

295 enrichment at 75% resulted in a decrease in beta-sheets with an increase in random structures, indic

296 8-alphaS fibrils consist of strongly twisted beta-sheets with an increased inter-beta-sheet distance

297 These proteins comprise cylindrical beta-sheets with long extracellular loops and create por

298 lysine, coassemble as stacks of antiparallel beta-sheets with precisely patterned charged lattices st

299 tional bacterial proteins and may use a core beta-sheet within an alpha+beta-fold to coordinate conse

300 of the materials and verify the presence of beta-sheets within the hybrid hydrogels.