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1  and acceptors at neutral pH and disrupt the alpha-helical conformation.
2 active mutations suggested that IL2 is in an alpha-helical conformation.
3 that MEM-265 may recognize the epitope in an alpha-helical conformation.
4 hat the apoE CT domain adopts an amphipathic alpha-helical conformation.
5 cent reports have suggested a propensity for alpha-helical conformation.
6 e previous predictions, this region is in an alpha-helical conformation.
7 binding of Zn(2+) in a pi-helical but not an alpha-helical conformation.
8 a very strong preference for a transmembrane alpha-helical conformation.
9  of transmembrane domains IV and V is in the alpha-helical conformation.
10     The pattern of accessibility suggests an alpha-helical conformation.
11  acid peptides bound GroEL in an amphipathic alpha-helical conformation.
12 he role of Gla4 in stabilizing the apo-con-T alpha-helical conformation.
13  constraining short peptides typically in an alpha-helical conformation.
14 ing a significant role in maintenance of the alpha-helical conformation.
15 a beta-turn from residues Arg6 to Arg9 or an alpha-helical conformation.
16 FE3 and is predicted to adopt an amphipathic alpha-helical conformation.
17 pha-subunits of Gi and Go in a predominantly alpha-helical conformation.
18 i + 4 positions have been shown to stabilize alpha-helical conformation.
19 trate that transmembrane domain XII is in an alpha-helical conformation.
20 provided additional evidence for a conserved alpha-helical conformation.
21 hown by peptide models to be specific to the alpha-helical conformation.
22 to the 1-28 peptide region when folded in an alpha-helical conformation.
23 eas membrane-bound alpha-synuclein adopts an alpha-helical conformation.
24 al mesophases in which the peptides adopt an alpha-helical conformation.
25 to the ER based on their ability to adopt an alpha-helical conformation.
26 ly charged lipid membranes while adopting an alpha-helical conformation.
27 inhibit beta conformations and stabilize the alpha-helical conformation.
28 G alpha s protein) of the peptide adopted an alpha-helical conformation.
29  does not discriminate between the 3(10)- or alpha-helical conformations.
30 roove-binding peptidic motifs known to adopt alpha-helical conformations.
31 f polypeptides under conditions that produce alpha-helical conformations.
32 c-containing M2 and correspond to more ideal alpha-helical conformations.
33 ut GdnHCl, the combined data are well fit by alpha-helical conformations.
34 rom sequences that do not spontaneously form alpha-helical conformations.
35 by stabilizing alpha-synuclein in an active (alpha-helical) conformation.
36 mphiphilic in the pi-helical, but not in the alpha-helical, conformation.
37 olution, the 6-10 residue peptides adopt the alpha-helical conformation; (3) there might be two inter
38  pH-dependent manner between a transmembrane alpha-helical conformation, a peripherally bound nonheli
39  accessibilities to molecular O(2) reveal an alpha-helical conformation along the sequence.
40 ontains approximately 50% of its residues in alpha-helical conformation and <10% in beta-structure.
41  simulations on the Abeta(42) monomer at its alpha-helical conformation and a pentamer fibril fragmen
42 EBP (residues 117-137) adopts a well defined alpha-helical conformation and binds 14-3-3 in a phospho
43                       The Rev peptide has an alpha-helical conformation and binds in the major groove
44    Interestingly, HCDR1 of MAb 3.1 adopts an alpha-helical conformation and engages in hydrophobic in
45 mplex revealed that EGL-1 adopts an extended alpha-helical conformation and induces substantial struc
46 ntion that transmembrane domain XII is in an alpha-helical conformation and on the periphery of the 1
47  several molecules of monomeric alphaS in an alpha-helical conformation and that such channels may ha
48 NBD consensus sequence is consistent with an alpha-helical conformation and that these residues maint
49 s show that W41F M2 retains the pH-dependent alpha-helical conformations and tetrameric structure of
50 hauser enhancement buildup points to a large alpha-helical conformation, and a distinct increase in f
51  the residues in them are found to be in the alpha-helical conformation, and another 10% in the 3(10)
52 ormation is the most stable, followed by the alpha-helical conformation, and then the unstructured co
53 ng PS revealed features characteristic of an alpha-helical conformation approximately approximately 1
54  Ac-(Aib)(4)-NH(2) constrained to 3(10)- and alpha-helical conformations are presented.
55               The peptide agonist retains an alpha-helical conformation as it sits deep within the re
56 h from a beta-turn/coil to an extended quasi-alpha-helical conformation as the actin-contacts are bro
57 h formation of a predominantly transmembrane alpha-helical conformation, as determined from the trans
58 ctivity of exon 4 may require adoption of an alpha-helical conformation, as mutations that disrupt al
59 w-concentration Con A transforms to a highly alpha-helical conformation at both neutral and low pH.
60 ordered state at low [TFE] and with a highly alpha-helical conformation at high [TFE].
61 E), or because of the appearance of a highly alpha-helical conformation at high TFE and hexafluoro-2-
62 that extended conformations are favored over alpha-helical conformations at the dipeptide level at an
63  formation of a H(+)-stabilized intermediate alpha-helical conformation before aggregation develops.
64  NS4A revealed that this region can adopt an alpha-helical conformation, but that this folding requir
65 of Abeta(42) peptide (residues 17-21) to its alpha-helical conformation by interacting specifically i
66 y binding to the HAP being stabilized in the alpha-helical conformation by the presence of water.
67 y labeled Ac-A(24)-NHCH(3) constrained to an alpha-helical conformation by use of property tensor tra
68 ta42 is predominantly disordered but samples alpha-helical conformations covering residues 15-24 and
69  inserted segment in the S1 domain adopts an alpha-helical conformation, despite being predicted to b
70 cular dichroism data showed that Hsn-5 in an alpha-helical conformation does not aggregate in a hydro
71                     Conantokin-Pr3 adopts an alpha-helical conformation even in the absence of divale
72 ains important residues which, in a putative alpha-helical conformation, exert inhibitory control on
73 the three MPER peptides each adopt symmetric alpha-helical conformations exposing the amino acid side
74 ary structure modeling algorithms predict an alpha-helical conformation for one of the gelsolin PPI-b
75 acts or may support the proper transmembrane alpha-helical conformation for optimal positioning of th
76 mbrane interior, which is consistent with an alpha-helical conformation for the four transmembrane do
77 a also indicate a possible minor increase in alpha-helical conformation for the receptor in the compl
78 the middle of the exon 9 peptide and a loose alpha-helical conformation for the rest of the peptide.
79 me time to maximize the active mdm-2 binding alpha-helical conformation for these peptides, each was
80                          Assuming the likely alpha-helical conformation for this area of the b subuni
81 attern of accessibility is consistent with a alpha-helical conformation for this segment of TMH6.
82    We found that SLN adopts a highly defined alpha-helical conformation from F9 through R27, with a b
83 n 1-17 upon membrane-association result in a alpha-helical conformation from K6 to F17, i.e., up to t
84 oth detergent systems, the peptide adopts an alpha-helical conformation from residue 4 through 18.
85 of helix 12, which can result in an extended alpha-helical conformation, further accelerates lipid-mi
86 e with incubation in a solvent that promotes alpha-helical conformation, further suggesting that conf
87 residues predisposing the peptide toward the alpha helical conformation in an effort to enhance the r
88 nt alpha-helical region and induces a unique alpha-helical conformation in Abeta.
89 nformation in neutral and basic media and an alpha-helical conformation in acidic media, the helical
90 21 are also embedded but deviate from linear alpha-helical conformation in contrast to I693-K716, whi
91 ane interaction and the novel membrane-bound alpha-helical conformation in IAPP aggregation are discu
92 d polypeptide chains, adopts a predominantly alpha-helical conformation in its native state.
93                                BM2 adopts an alpha-helical conformation in lipid membranes.
94         Moreover, N34(L6)C28 adopts a highly alpha-helical conformation in lipid vesicles.
95    Here we show that helices 6-8 maintain an alpha-helical conformation in membranes with a lipid com
96 t potent stapled peptide, DD5-o, revealed an alpha-helical conformation in methanol, stabilized by an
97 tions were on the hydrophilic face showed an alpha-helical conformation in mild buffer.
98 nd to have a strong tendency for adopting an alpha-helical conformation in solution.
99 peptide, prove that the peptide is in an all alpha-helical conformation in the bilayers of multilamel
100  energy conformation was found to exhibit an alpha-helical conformation in the cyclized address seque
101                     It was suggested that an alpha-helical conformation in the cyclized address seque
102 inal transmembrane domain of CYPOR adopts an alpha-helical conformation in the lipid membrane environ
103 that the MSD peptide assumes a stable tilted alpha-helical conformation in the membrane.
104 of RGS4 revealed that the peptide adopted an alpha-helical conformation in the presence of anionic ph
105 ructured in solution and only folded into an alpha-helical conformation in the presence of liposomes.
106  impairment of the nitrated protein to adopt alpha-helical conformation in the presence of liposomes.
107 ve residues has the propensity to take on an alpha-helical conformation in the presence of SDS micell
108 eous solution at neutral pH but can adopt an alpha-helical conformation in the presence of the hydrop
109  aggregation and displayed approximately 70% alpha-helical conformation in the presence of urea and S
110 ical conformation in CDCl(3) solution and an alpha-helical conformation in the solid state.
111 no acids 21-45 and 139-164 tended towards an alpha-helical conformation in trifluoroethanol buffer, i
112 all proteins have a strong tendency to adopt alpha-helical conformation in trifluoroethanol.
113 length; both peptides adopt nearly identical alpha-helical conformations in the complexes, where the
114               Conantokins-Pr1 and -Pr2 adopt alpha-helical conformations in the presence of divalent
115 PrP(89-143) form a mixture of beta-sheet and alpha-helical conformations in the randomly aggregated s
116 t bZIP-bRs have quantifiable preferences for alpha-helical conformations in their unbound monomeric f
117             Many host-defense peptides adopt alpha-helical conformations in which cationic side chain
118 d that when kafirin was dissolved in GAA its alpha-helical conformation increased substantially.
119 ecular association, whereas stabilization of alpha-helical conformation inhibits beta-sheet formation
120 smaller binding affinity and thus stabilizes alpha-helical conformations intermediately between NaClO
121 ransition of the F198S variant from a normal alpha-helical conformation into an oligomeric beta-sheet
122 t occur from cellular allowed random coil or alpha-helical conformation into insoluble cell-deleterio
123                       In SDS, an increase in alpha-helical conformation is indicated by the predomina
124 osphorylation, suggesting that the predicted alpha-helical conformation is involved in the inhibition
125 he other helical polyamino acids in that its alpha-helical conformation is most stable in the left-ha
126           Previously, we have shown that the alpha-helical conformation is one of the important struc
127  of the kafirin molecules in GAA, assuming a alpha-helical conformation may have enhanced water bindi
128 e that conditions that promote weakly stable alpha-helical conformations may promote IAPP aggregation
129 e Trp to Phe(CN) mutation alters neither the alpha-helical conformation nor the 4-helix bundle struct
130 ues 176-227), retaining the disulfide-linked alpha-helical conformation observed in the normal cellul
131                                          The alpha-helical conformation occurred only after the forma
132 show for the first time that MOZ DPF induces alpha-helical conformation of H3K4-T11, revealing a uniq
133 ce loop (V63-N72) appear to be flexible; the alpha-helical conformation of helix B (E17-F22) is absen
134  is presented that stabilizes a pre-amyloid, alpha-helical conformation of IAPP.
135                                           An alpha-helical conformation of PAP(248-286), lying parall
136 the chemical chaperones act to stabilize the alpha-helical conformation of PrP(C) and thereby prevent
137 conformational change from the predominantly alpha-helical conformation of PrP(C) to the PrP(Sc) stat
138 Salmonella typhimurium indicates a generally alpha-helical conformation of the linker region, and a c
139 te that phosphorylation at T3 stabilizes the alpha-helical conformation of the N-terminal 17 amino ac
140 ), which promotes shell assembly, the highly alpha-helical conformation of the P8 subunit is stabiliz
141                            The predominantly alpha-helical conformation of the peptide alone at pH5-6
142                            The propensity to alpha-helical conformation of the peptides in amphipathi
143 an engineered metal ion site, stabilizing an alpha-helical conformation of this loop segment.
144  bridge is believed to stabilize an extended alpha-helical conformation of this peptide while in solu
145 hypotheses for the high thermal stability of alpha-helical conformations of alanine-based peptides by
146                     We conclude that the non-alpha-helical conformations of these peptides are domina
147 f the region, which is predicted to adopt an alpha-helical conformation on membrane contact.
148 ther phage proteins to nucleate pVIII in the alpha-helical conformation on the DNA.
149 mmonly assumed model where alphaS lies in an alpha-helical conformation on the membrane surface and i
150 -TM region systematically prefers a straight alpha-helical conformation once embedded in a membrane b
151  binds as a dimer to the dodecapeptide in an alpha-helical conformation, predicated on a substantial
152  a transition of prion protein (PrP) from an alpha-helical conformation, PrP(C), to a beta-sheet-rich
153 nd Glu30-Lys33 lactam rings were favoring an alpha-helical conformation rather than a turn, we introd
154 ated that residues 306-314 were in a regular alpha-helical conformation representing the end of helix
155 tion capability (up to 5-fold) by fixing the alpha-helical conformations required for optimal recepto
156 ody and base primarily in beta-structure and alpha-helical conformations, respectively.
157           The dipole moments associated with alpha-helical conformations show the best alignment with
158 o side-chain lactam rings would stabilize an alpha-helical conformation shown to be important for the
159 o-side-chain lactam rings would stabilize an alpha-helical conformation shown to be important for the
160 ocidin is predicted to assume an amphipathic alpha-helical conformation similar to many other linear
161 e TNFalpha-derived sequence was induced into alpha-helical conformation, suggesting that conformation
162 backbone of TRH inside the receptor is in an alpha-helical conformation, suggesting that the receptor
163 tions had similar FTIR spectra, with greater alpha-helical conformation, than the kafirin preparation
164 bacterial surface, where this peptide adopts alpha-helical conformations, than cholesterol-enriched L
165 lar, the peptides assume a membrane-spanning alpha-helical conformation that does not disrupt bilayer
166 into eukaryotic cells adopts a well-ordered, alpha-helical conformation that packs tightly against th
167 s a delicate balance to maintain pVIII in an alpha-helical conformation that requires either an orien
168 ore likely than the false positives to adopt alpha-helical conformations that transition to loops at
169 re pHLIP adopts a well-defined transmembrane alpha-helical conformation the peptide still exhibits he
170 gment of the peptide takes on a well-defined alpha-helical conformation; the center segment of the pe
171 cate that the transmembrane segment is in an alpha-helical conformation throughout, with an average h
172 0-204 and 215-223) undergo a transition from alpha-helical conformation to a beta and/or random coil
173 ulted in a time-dependent transition from an alpha-helical conformation to a beta-sheet structure and
174 led the binding of a C-terminal extension in alpha-helical conformation to a pocket next to the activ
175 present direct evidence of a conversion from alpha-helical conformation to beta-sheet fibrils in the
176                        DAXX uses an extended alpha-helical conformation to compete with major inter-h
177 bind CD4, but the constructs must display an alpha-helical conformation to do so.
178 somer (PrPSc), shifting from a predominantly alpha-helical conformation to one dominated by beta-shee
179           Complexin binds in an antiparallel alpha-helical conformation to the groove between the syn
180 nomenclature) of Cgb adopts a highly ordered alpha-helical conformation unlike any previously charact
181 olution is largely unstructured, acquires an alpha-helical conformation upon association with lipid m
182 t up to six additional residues may adopt an alpha-helical conformation upon binding actin.
183                             It folds into an alpha-helical conformation upon binding to anionic (but
184  coil conformation in solution and adopts an alpha-helical conformation upon binding to lipid membran
185 inear cationic peptides adopt an amphipathic alpha-helical conformation upon binding to lipids as an
186 lein is natively unstructured but assumes an alpha-helical conformation upon binding to phospholipid
187 f the c-region of the signal peptide form an alpha-helical conformation upon binding to SecA.
188 peptides, most of which adopt an amphipathic alpha-helical conformation upon binding to the lipids.
189                        The peptide adopts an alpha-helical conformation upon binding to the minichape
190 e N-terminus of the protein, which adopts an alpha-helical conformation upon lipid binding, is essent
191 abilization of linear diazido peptides in an alpha-helical conformation upon reaction with dialkynyl
192 y and confirmed that 2 bound to copper in an alpha-helical conformation via its two histidine side ch
193 with thioflavin T, while with SDS, a partial alpha-helical conformation was adopted that gave no fluo
194 ilization and reconstitution an ~10% loss of alpha-helical conformation was observed, which may refle
195 ogy for stabilizing a peptide in a bioactive alpha-helical conformation, we report the discovery of a
196 y revealed that the signal peptide adopted a alpha-helical conformation when bound by NapD, and subst
197 de is unstructured in solution, it adopts an alpha-helical conformation when bound to the ECD.
198  IAPP(1-19) is conformationally stable in an alpha-helical conformation when bound to the membrane.
199 members (urotensins and sauvagine) assume an alpha-helical conformation when interacting with CRF rec
200 30),Lys(33),Nle(38)]hCRF((12-41))] assume an alpha-helical conformation when interacting with their r
201 sition, adopting an L-shaped, extended chain/alpha-helical conformation when it interacts with a phyl
202 solution, but strongly adopts an amphipathic alpha-helical conformation when partitioned into membran
203 ratin bound to the membrane interface in the alpha-helical conformation when the peptide/lipid (P/L)
204 ution but undergoes a concerted change to an alpha-helical conformation when the polarity of the envi
205          However, wt-alphaSyn(2SS) adopts an alpha-helical conformation, whereas A30P-alphaSyn(2SS) a
206         Lowering the pH favors the monomeric alpha-helical conformation, whereas increasing the ionic
207  insert into the bilayers in a predominantly alpha-helical conformation, whereas self-associated fusi
208              Folding of this peptide into an alpha helical conformation, which occurs upon binding to
209         Interestingly, the peptide adopts an alpha-helical conformation, which orients the motif resi
210 mplex formation, the CaMKI peptide adopts an alpha-helical conformation, while changes in the CaM dom
211 arting at the N-terminus of alphaS adopts an alpha-helical conformation, while succeeding residues re
212 s of both peptides were observed to be in an alpha-helical conformation, while the N-terminal halves
213 ttern of accessibility is consistent with an alpha-helical conformation with a wide angle of accessib
214 istent with the notion that the TMs 6 are in alpha-helical conformations with a narrow strip of acces
215 ater solution into thermodynamically stable, alpha-helical conformations with well-defined tertiary s
216 elles, alphaS adopts an extended amphipathic alpha-helical conformation, with its long axis aligned w
217 opy showed that the channel exists mostly in alpha-helical conformation, with more than 50% alpha-hel
218 ured in an aqueous environment but adopts an alpha-helical conformation within a localized region on
219 21, an interaction necessary for stabilizing alpha-helical conformation within the transactivation do
220 sulfone groups resulted in disruption of the alpha-helical conformations without loss of water solubi
221 on cross-linking strategy to reinforce their alpha-helical conformation, yielding improved protease r

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