ライフサイエンスコーパス: polypeptide backbone

1 drophobic moieties and groups located on the polypeptide backbone).

2 rgetic cost associated with solvation of the polypeptide backbone.

3 EM effect is most likely due to 14N from the polypeptide backbone.

4 ns near the N terminus and C terminus of the polypeptide backbone.

5 e groups remain embedded directly within the polypeptide backbone.

6 ains for each chain, where the S-S spans the polypeptide backbone.

7 anization of glycans that decorate the mucin polypeptide backbone.

8 ns to position the charges distally from the polypeptide backbone.

9 dation process, which causes cleavage of the polypeptide backbone.

10 idues, thereby adding an extra carbon to the polypeptide backbone.

11 in the formation of a deep trefoil knot in a polypeptide backbone.

12 ancer-related antigens displayed on a single polypeptide backbone.

13 step to produce an acylimine linkage in the polypeptide backbone.

14 x and a minority state of locally disordered polypeptide backbone.

15 ric interactions between side chains and the polypeptide backbone.

16 changes involve substantial ordering of the polypeptide backbone.

17 ions and is lined by carbonyl oxygens of the polypeptide backbone.

18 the first 30 amino acids within the E1A 1-80 polypeptide backbone.

19 cant alterations in the conformations of the polypeptide backbones.

20 n the extent of sugar modifications of their polypeptide backbones.

21 ts cannot be classified as good solvents for polypeptide backbones.

22 quences without the geometric constraints of polypeptide backbones.

23 tides must originate, at least partially, in polypeptide backbones.

24 ins and is a useful model system for generic polypeptide backbones.

25 t temperatures is a poor solvent for generic polypeptide backbones.

26 the selectivity filter residues, rather than polypeptide backbones.

27 rea, packing angle, and distance between the polypeptide backbones.

28 Although the MSP1a polypeptide backbone alone was adherent to tick cell ext

29 cross cell membrane, the isotope exchange of polypeptide backbone amide hydrogens of hemoglobin was c

30 MR dynamics studies have been undertaken for polypeptide backbone amide N-H bond vectors for both the

31 inewidths of Raman bands associated with the polypeptide backbone (amide I) exhibit progressive narro

32 Our results show that the majority of the polypeptide backbone amino acid residues of deoxy- and c

33 riences diminished hydrogen bonding with the polypeptide backbone, an Asp at position 3 forms a biden

34 e divided into two sub-problems, placing the polypeptide backbone and adding side-chains.

35 The polypeptide backbone and buried side chains are well ord

36 t the magic angle spectra show that both the polypeptide backbone and His(37) side chain are more con

37 gen bonding interaction between the enzyme's polypeptide backbone and its substrate.

38 m accepts three hydrogen bonds, two from the polypeptide backbone and one from the positively-charged

39 r example, how and why did nature select the polypeptide backbone and proteinaceous side chains?

40 ons between O, N, and C unified atoms of the polypeptide backbone and side chains.

41 own how the spatial relationship between the polypeptide backbone and the DNA helps to determine what

42 nges in the spatial relationship between the polypeptide backbone and the DNA.

43 perturbation of a deeply buried part of the polypeptide backbone and to protonation of a carboxylic

44 side-chain imposes severe constraints on the polypeptide backbone, and thus it seems likely that it p

45 dies showed that water is a poor solvent for polypeptide backbones, and therefore, backbones form col

46 and also increased the extent to which PRPg polypeptide backbones are modified by a GAG chain.

47 recognition of the central importance of the polypeptide backbone as a determinant of protein conform

48 hydrophobic groups--a result that holds for polypeptide backbones as well.

49 known to stabilize hydrogen bonds within the polypeptide backbone, as analyzed by circular dichroism

50 e catalyzes the UV-dependent cleavage of the polypeptide backbone at both the LSGGQ motif and the nuc

51 A concurrent turn of the polypeptide backbone at Phe-245 moves the rest of the ca

52 o form a new six-membered ring, cleaving the polypeptide backbone at the 65-66 position.

53 onding interactions from 1 aa side chain and polypeptide backbone atoms of the antibody light and hea

54 cted by the sequence of sidechains along the polypeptide backbone, but despite this the developement

55 Here, we ask if polypeptide backbones can intrinsically undergo the requ

56 ding sites for the cations are formed by the polypeptide backbone carbonyl groups tilting away from t

57 Both structures permit full tracing of the polypeptide backbone chain from residues 4-356, includin

58 2+)/calmodulin activation of the kinase, the polypeptide backbone chain of myosin light chain kinase

59 The polypeptide backbone chain was traced by examination of

60 ns via multiple mechanisms that lead to both polypeptide backbone cleavage events and side chain modi

61 filaments in a single tomogram revealed the polypeptide backbone conformation and filament polarity

62 The role of polypeptide backbone conformation in the formation of ma

63 RMM36m, with improved accuracy in generating polypeptide backbone conformational ensembles for intrin

64 The polypeptide backbone conformations and the side-chain or

65 n of a photosensitive beta-turn mimic in the polypeptide backbone, consisting of a newly designed azo

66 and straight phi,psi angles assignments, and polypeptide backbone coordinates.

67 A high degree of polypeptide backbone desolvation, and not the formation

68 The polypeptide backbone displayed a single circular dichroi

69 The polypeptide backbone dynamics of acid-unfolded apomyoglo

70 exchange (H/DX) has been used to define the polypeptide backbone dynamics of full-length methyl CpG

71 The conformational propensities and polypeptide backbone dynamics of this state have been ch

72 itored within the amide I' absorbance of the polypeptide backbone exhibit two distinct kinetics phase

73 nitored within the amide I absorbance of the polypeptide backbone exhibit two distinct relaxation pha

74 The polypeptide backbone exhibits a 2-fold axis of quasi-sym

75 YiaK has a new polypeptide backbone fold and a novel mode of recognizin

76 This protease has a unique polypeptide backbone fold and contains a novel Ser-His-H

77 that the BEACH domain has a new and unusual polypeptide backbone fold, as the peptide segments in it

78 resolution, and show that it possesses a new polypeptide backbone fold.

79 The polypeptide backbone folds into a large right-handed cyl

80 ontent modulates the intrinsic preference of polypeptide backbones for collapsed structures.

81 near the center of the octamer site, and its polypeptide backbone forms a pair of hydrogen bonds with

82 In each subunit the polypeptide backbone forms large beta-sheets and enclose

83 The polypeptide backbone forms transient, sparse hydrogen-bo

84 by low hemolytic activity, and protects the polypeptide backbone from proteolytic degradation.

85 kage between the proximal histidines and the polypeptide backbone has been broken and to characterize

86 ins in which the chemical composition of the polypeptide backbone has been partially altered; and pro

87 ary structures and pendant glycosides on the polypeptide backbone have sparked lots of research inter

88 eveal that UPRTase recognizes uracil through polypeptide backbone hydrogen bonds to the uracil exocyc

89 pronounced expansion and contraction in the polypeptide backbone, i.e., to be photoelastic.

90 actor and the amide hydrogen of the adjacent polypeptide backbone in all three oxidation states.

91 The root mean square deviation of the polypeptide backbone in the complex is 2.07 A.

92 ar [(1)H]-(15)N NOEs show that, although the polypeptide backbone in the H helix region is more flexi

93 n water leading to an intrinsic expansion of polypeptide backbones in the absence of denaturants.

94 cies and Ramachandran dihedral angles of the polypeptide backbone indicates the nature of the beta-sh

95 The role of polypeptide backbone interactions in 4-oxalocrotonate ta

96 Unlike in Rtms5, in the native protein the polypeptide backbone is cleaved between Cys62 and Met63.

97 A virtual polypeptide backbone is created by joining consecutive C

98 eins have folded configurations in which the polypeptide backbone is knotted.

99 The folding of the polypeptide backbone is nearly identical with that of tu

100 in a dimer run in parallel, and that (b) the polypeptide backbone is relatively rigid and inflexible

101 t with an increase in the flexibility of the polypeptide backbone leading to a decreased probability

102 shaft motions along the entire length of the polypeptide backbone manifested by the anticorrelation o

103 g that similar O-glycan ligands on different polypeptide backbones may be common death trigger recept

104 This strongly indicates that there are polypeptide-backbone motions activated at room temperatu

105 BTD) and is designed to be embedded within a polypeptide backbone, not attached as part of a conforma

106 ded by free rotation around the bonds of the polypeptide backbone of a few amino acid residues, but d

107 f attachment of carbohydrate moieties to the polypeptide backbone of a second mycobacterial glycoprot

108 magnetic resonance (NMR) assignments for the polypeptide backbone of a tetrameric N-terminal fragment

109 pproximately 50% of the amide protons of the polypeptide backbone of Abeta(1-40) resist exchange in a

110 This model places the polypeptide backbone of both the first and third Ca2+-bi

111 of altering the carbohydrate moieties or the polypeptide backbone of GspB.

112 of lactase and phlorizin active sites in the polypeptide backbone of LPH-D1796fs and LPH-Y1473X respe

113 lative rates of exchange of hydrogens of the polypeptide backbone of PE with deuterium atoms from D(2

114 ymerize rapidly at 100 degrees C to give the polypeptide backbone of PNA.

115 e diphosphates leads to fragmentation of the polypeptide backbone of R1.

116 ational coupling pathway, which, through the polypeptide backbone of the beta subunit, physically lin

117 Some positional changes in the polypeptide backbone of the beta6-beta10-beta9 sheet con

118 e K is able to complete the digestion of the polypeptide backbone of the DNA oligonucleotide-linked t

119 rbohydrates based upon the properties of the polypeptide backbone of the maturing substrate.

120 axation parameters of pXqua confirm that the polypeptide backbone of the QUA2 region is more dynamic

121 alone or tethered to D1, indicating that the polypeptide backbone of this part of D2 is highly flexib

122 er enhanced by small (<3 A) movements in the polypeptide backbones of certain antibody CDR loops, by

123 ious study, provide strong evidence that the polypeptide backbones of the head domains form a symmetr

124 led sigma protein is then used to cleave the polypeptide backbones of the RNAP proteins at exposed re

125 proximate twofold symmetry axis relating the polypeptide backbones of these two helix-turn-helix unit

126 ith a glutathione-responsive self-assembling polypeptide backbone (PEP1), a DOTA chelator, and an int

127 onservation of the binding site on the nAChR polypeptide backbone per se.

128 d homologs indicate that the knot within the polypeptide backbone plays a significant role in the bio

129 Here we measure intramolecular polypeptide backbone reconfiguration as a way to underst

130 utation at position 82 induces change in two polypeptide backbone regions, 35-41 and 67-68, which may

131 The time scale for ordering of the polypeptide backbone relative to the side chains is a cr

132 dated the different nucleotides, whereas the polypeptide backbone remained similar among the structur

133 Instead, polypeptide backbones sample conformations that are dena

134 nd its digestion with PNGase F resulted in a polypeptide backbone similar in size to salivary CA VI.

135 denaturation and induced alterations in MHC polypeptide backbone structure as determined by circular

136 onsistent with the absence of a well-defined polypeptide backbone structure in this region of the pro

137 , a betabetaalpha protein motif based on the polypeptide backbone structure of a zinc finger domain.

138 the kinetics of amide H/D exchange along the polypeptide backbone suggest that the monomer has a glob

139 ering the active site from a position on the polypeptide backbone that is not utilized in other tyros

140 induced a local conformational change in the polypeptide backbone that resulted in a narrowed S1 subs

141 e marked structural homology of the selectin polypeptide backbones, the selectin EGF surfaces show un

142 lize polypeptides through exclusion from the polypeptide backbone; the inhibition of renaturation/rea

143 the amino acid building units along a common polypeptide backbone to maximise their performance.

144 re incorporated as redox-active groups along polypeptide backbones to function as anode and cathode m

145 allows placement of a variety of probes on a polypeptide backbone, to monitor the behavior of labeled

146 ns such as SCN(-) and I(-) interact with the polypeptide backbone via a hybrid binding site that cons

147 In contrast, the half-life of the polypeptide backbone was 8 h, indicating that palmitoyla

148 The folding status of each segment of the polypeptide backbone was determined from the deuterium l

149 urospora crassa Cu(6)-metallothionein (NcMT) polypeptide backbone was determined using homonuclear, m

150 ely in the nuclear fraction, and size of its polypeptide backbone was the same as that of the cytopla

151 ay influence the conformational options of a polypeptide backbone, we have characterized Pro-->Ala mu

152 eover, slower internal motional modes of the polypeptide backbone were identified by measuring transv

153 m appears to contain "random" buried runs of polypeptide backbone which convert to alpha-helix in the

154 upon the reaction of Thr 66 Ogamma with the polypeptide backbone, which in turn reduces the conjugat

155 ocessively and directionally steps along the polypeptide backbone with a kinetic step size of approxi

156 ministrated clinically, erythropoietin has a polypeptide backbone with complex dishomogeneity in its

157 ider how the position and orientation of the polypeptide backbone (with respect to the DNA) helps to

158 mitted the 3D structure determination of the polypeptide backbone without the substitution and utiliz