ライフサイエンスコーパス: polyalanine

1 cid residues of the C subunit are modeled as polyalanine.

2 ues that resulted from a duplication of nine polyalanines.

3 greement with J-coupling constants for short polyalanines.

4 Two of the models (polyalanine (37A) and superoxide dismutase 1 (SOD1) muta

5 alpha-helices, and 3(10)-helices for capped polyalanines, acetyl(ala)(N)()NH(2), for values of N fro

6 free energy landscape coordinate of a mainly polyalanine alpha-helical peptide, AP of sequence AAAAA(

7 y terms that contribute to the transfer of a polyalanine alpha-helix from the aqueous phase into lipi

8 nscripts results in the accumulation of SCA8 polyalanine and DM1 polyglutamine expansion proteins in

9 The long stretches of polyalanine and glycine-alanine subrepeats, which accoun

10 ucidate the methodology using the folding of polyalanine, and demonstrate that its alpha-helix foldin

11 structs express homopolymeric polyglutamine, polyalanine, and polyserine proteins in the absence of a

12 shift anisotropies are intrinsic to helical polyalanines, and a correcting L-R-based model is introd

13 system of properly water-solubilized, spaced polyalanines are presented.

14 The 21 residue polyalanine-based F(s) peptide was studied using thousan

15 In the present study, polyalanine-based peptides (i.e., derived from Ac-KA14K-

16 ous reports of conformational preferences in polyalanine-based peptides including (i) terminal 3(10)-

17 glycine-rich matrix and not the crystalline, polyalanine beta-sheets.

18 We also show that long polyalanines can protect against a pro-apoptotic stimulu

19 the study of two model systems, a 15-residue polyalanine chain and the R2-fragment ((273)GKVQIINKKLDL

20 We also explore off-lattice polyalanine chains that yield surprisingly similar resul

21 l displacements and numerical simulations of polyalanine chains.

22 We find that polyalanine closely approximates a random coil with excl

23 by molecular replacement using superimposed polyalanine coordinates of six intracellular lipid-bindi

24 ed between solubilizing lysine regions and a polyalanine core permit rigorous characterization of con

25 ibrium is related to the length scale of the polyalanine crystallites.

26 The resulting polyalanine-derived, quantitative propensity sets expres

27 h), is a 21 bp in-frame duplication within a polyalanine-encoding region at the 5'-end of the Hoxd13

28 rent proteins with long polyglutamines and a polyalanine-expanded protein, and reduces their toxicity

29 ystrophy mouse model expressing an authentic polyalanine-expanded protein.

30 how that this aggregate-prone protein with a polyalanine expansion can also protect against polygluta

31 phy (OPMD) is a late onset disease caused by polyalanine expansion in the poly(A) binding protein nuc

32 A short abnormal polyalanine expansion in the polyadenylate-binding prote

33 g binding to WT PHOX2B and a CCHS-associated polyalanine expansion mutant but only weakly or not at a

34 a late-onset muscular dystrophy caused by a polyalanine expansion mutation in the coding region of t

35 resented, each heterozygous for a documented polyalanine expansion mutation in the PHOX2B gene and ev

36 ed as an autosomal dominant disorder and the polyalanine expansion mutation is thought to confer a to

37 have the mildest of the CCHS-related PHOX2B polyalanine expansion mutations, coding for only five ex

38 -prone proteins with either polyglutamine or polyalanine expansions in Drosophila.

39 Polyalanine expansions in the 20-residues region of the

40 Polyalanine expansions in two of three large imperfect t

41 , we investigated the effects of the longest polyalanine expansions on the homeodomain-mediated nucle

42 Mutations, principally leading to polyalanine expansions within the protein, have been fou

43 dystrophy (OPMD), a disorder caused by small polyalanine (GCG) expansions in the gene that codes for

44 conformations of protonated polyglycine and polyalanine (Gly(n)H and Ala(n)H+, n = 3-20) in the gas

45 Two configurations of a membrane-bound 25mer polyalanine helix were found to be lower in free energy

46 s of cysteines in three model systems: (a) a polyalanine helix, (b) the isolated C helix (residues 53

47 We found that fibril formation for polyalanines incorporate features that are characteristi

48 helices become relatively more stable as the polyalanines increase in size.

49 ast iso-1-cytochrome c variants that contain polyalanine inserts ranging from 6 to 30 residues in len

50 Here, we report FRET results on gas-phase polyalanine ions obtained by measuring FRET efficiency t

51 hase 3(10)-helices are more stable for small polyalanines, largely due to the additional H-bond, the

52 We fitted a polyalanine-level model to all 3,757 ordered residues in

53 We were able to build near-complete polyalanine-level models of the eIF3 PCI/MPN core and of

54 a variant that contains an eight-amino-acid polyalanine-like helix stabilised by a Glu-Arg salt brid

55 Helix-coil transitions in polyalanine molecules of length 10 are studied by multi-

56 esidues that is complementary to the helical polyalanine N-terminus.

57 and H9 were either removed or substituted by polyalanine or polyleucine.

58 We examine a 21-amino acid, mainly polyalanine peptide and calculate the free energy along

59 By pushing a polyalanine peptide onto a polar surface, simulations re

60 icantly higher than the T(m) of a 21-residue polyalanine peptide, A(21).

61 surements have been performed for protonated polyalanine peptides (A10 + H+, A15 + H+, A20 + H+, A25

62 n integrals for both the polyglycine and the polyalanine peptides are consistent with a self-solvated

63 Additionally, some of these polyalanine peptides are recognized by T cell lines gene

64 charged anchor residue is so pronounced that polyalanine peptides containing a single Asp can bind to

65 Systems containing 12-96 model polyalanine peptides form fibrils at temperatures greate

66 s, recent NMR experiments suggest that short polyalanine peptides in water populate the polyproline I

67 Thermal studies show that polyalanine peptides with minimal anchors and nearly all

68 ortunity to examine the unfolding process in polyalanine peptides.

69 the conformations of large multiply charged polyalanine peptides.

70 polypeptide complexes (RNCs) with different polyalanine (poly-A) inserts or signal peptides from mem

71 Polyalanine (poly-A) tracts exist in 494 annotated prote

72 e cell death associated with the poly(Q) and polyalanine [poly(A)] expansions.

73 Recently, polyalanine (polyA) tract expansions in the Aristaless-r

74 proteins with expansions in their endogenous polyalanine (polyA) tracts.

75 t different classes of calibrants, including polyalanine (PolyAla), tetraalkylammonium salts (TAA), a

76 ipid-bound form; the chimeric construct with polyalanine produced lower enthalpy gain.

77 Polyalanine proteins may also be present in the tissue o

78 argeted to the antisense FMR polyproline and polyalanine proteins selectively stain nuclear and cytop

79 s, generating polyproline, polyarginine, and polyalanine proteins, respectively.

80 Solubilized, isolated polyalanines provide optimal tools for testing polypepti

81 by polymerase chain reaction for the common polyalanine repeat expansion.

82 nonsense, and frameshift mutations, and 170 polyalanine repeat mutations were identified in 184 CCHS

83 yalanine repeat group compared to those with polyalanine repeat mutations.

84 CHS largely involve expansions of the second polyalanine repeat within the C-terminus of the protein,

85 Thus, expansions in all three large HOXA13 polyalanine repeats can cause HFGS.

86 don pairs that are least repetitive code for polyalanine repeats.

87 otifs that strongly resemble the crystalline polyalanine-rich and amorphous glycine-rich regions of s

88 nd 60 degrees C in water for the solubilized polyalanine series Ac-Hel-A(n)-(t)LInp(2)K(4)W-NH(2) of

89 hands and feet, is caused by expansions of a polyalanine stretch in the amino-terminal region of HOXD

90 The mutations identify the polyalanine stretch outside of the DNA binding domain of

91 uence of the black widow MiSp1-like revealed polyalanine stretches interrupted by glycine residues an

92 However, polyserine blocks and short polyalanine stretches were highly iterated within the pr

93 tion of EGFP/proSP-C21 constructs containing polyalanine substitution for Glu11-Thr18, 13PPDY16, or 1

94 ic increases in basal ATPase activity, (iii) polyalanine substitution of a helical connector segment

95 of alpha13 via the addition of a C-terminal polyalanine tail.

96 eries of solubilized, spaced, highly helical polyalanines that are N-capped by the optimal helix stab

97 stimulus or the toxicity caused by the long polyalanines themselves.

98 The CD response of these polyalanines to variations in temperature and salt or de

99 mice to expand the size of the third largest polyalanine tract by 10 residues (HOXA13(ALA28)).

100 PABPN1 with an expanded polyalanine tract forms aggregates consisting of tubular

101 teins, exclude the direct involvement of the polyalanine tract in dimer formation, and indicate that

102 ferent-sized expansions of an amino-terminal polyalanine tract in HOXD13.

103 gene that results in an N-terminal expanded polyalanine tract in polyA-binding protein nuclear 1 (PA

104 lear 1 gene (PABPN1), leading to an expanded polyalanine tract in the mutated protein.

105 Short expansions of the polyalanine tract in the N-terminus of PABPN1 lead to oc

106 7)] on the X chromosome, expanding the first polyalanine tract of the interneuron-specific transcript

107 ; in family 4, an expansion of an N-terminal polyalanine tract produces a similar phenotype; in famil

108 PMD is caused by the abnormal expansion of a polyalanine tract within the coding region of polyA bind

109 isease caused by the abnormal expansion of a polyalanine tract-encoding (GCG)(n) trinucleotide repeat

110 un; one domain resides within two N-terminal polyalanine tracts, and the other is present within the

111 ncluding proteins with long polyglutamine or polyalanine tracts, cause human diseases.

112 ent kindreds were found to have an identical polyalanine triplet repeat expansion ([GCG](9)) in the P

113 ystrophy (OPMD) is a rare myopathy caused by polyalanine triplet repeat expansion in the gene for pol

114 basis for the similar behavior of loops with polyalanine versus polyglycine inserts is discussed in t

115 y sequence of ECP-2, but scattered blocks of polyalanine were present, along with a C terminus rich i

116 (JPH3), potentially encoding polyleucine and polyalanine, whereas on the strand antisense to JPH3, th