ライフサイエンスコーパス: solvent exposure

1 ibit different RAs in response to changes in solvent exposure.

2 le Trp701 displayed an intermediate level of solvent exposure.

3 quencies consistent with a greater degree of solvent exposure.

4 ions in terms of interchain interactions and solvent exposure.

5 nsity score (OR 2.9, 95% CI 1.2-7.1) for any solvent exposure.

6 al methionines are directly related to their solvent exposure.

7 evaluation of the nervous-system effects of solvent exposure.

8 y and invariant residues tend to exhibit low solvent exposure.

9 ntration favoring conformations with greater solvent exposure.

10 a6, increasing the S-adenosylmethionine site solvent exposure.

11 c cluster that sequesters these H-bonds from solvent exposure.

12 consistent with P-cluster fragmentation and solvent exposure.

13 is effect revealed no obvious correlation to solvent exposure.

14 g surface is highly charged, consistent with solvent exposure.

15 terval = 0.89, 3.73), an indication of daily solvent exposure.

16 mine changes of Tyr and Trp environments and solvent exposures.

17 ilter's (1) histidine protonation state, (2) solvent exposure, (3) oligomeric state (the number of pr

18 e invasive breast cancer was associated with solvent exposure among clinical laboratory technologists

19 , 4.56) in the highest quartile of nonhexane solvent exposure and 1.62 (95% CI: 0.97, 2.72) in the hi

20 ed bases A1492 and G530 results in increased solvent exposure and an uncompensated loss of hydrogen b

21 elices, characteristic repeating patterns of solvent exposure and burial are observed.

22 er ATP or ADP, phosphorylation increased the solvent exposure and decreased the polarity of the envir

23 id isomerization rates can be predicted from solvent exposure and flexibility as determined by molecu

24 in which Trp residues had a higher degree of solvent exposure and fluorescence quenching.

25 dual spectral segment centroids, compared to solvent exposure and hydrogen bonding predictions and re

26 K4, K10, E15, E19, N35, N40, and E42, due to solvent exposure and low packing density.

27 Both solvent exposure and probe motions of ANSmal are enhance

28 ) which shields the side chain of Trp25 from solvent exposure and produces ring current shifts as lar

29 An arginine gateway opens, allowing solvent exposure and protonation of the chromophore's ph

30 ns alter the site-specific microenvironment, solvent exposure, and conformational flexibility of the

31 subdomain to probe its secondary structure, solvent exposure, and protein-protein interactions.

32 risingly, NMR chemical shifts, site-resolved solvent exposure, and relaxation studies show that the c

33 explained by the latter's deeper burial from solvent exposure, and stronger interaction with the carb

34 nteraction with NFkappaB, which controls its solvent exposure, and we demonstrate that this regulatio

35 d series of electrical measurements, optical/solvent exposures, and X-ray photoelectron spectroscopy.

36 Kinetics of solvent exposure are now known for nearly all backbone N

37 These results are consistent with solvent exposure as a major determinant of hydroxyl radi

38 Residue pairs were classified according to solvent exposure as well as by whether their backbone NH

39 of Arc-L1-Arc and wild-type Arc have similar solvent exposures as measured by the urea dependencies o

40 ombin interface and to screen for changes in solvent exposure at distant sites.

41 at proteins by controlling the chemistry and solvent exposure at their terminal interfaces.

42 ed spectroscopic probes of the structure and solvent exposure at these positions.

43 oid antagonists induce red shifts reflecting solvent exposure at this position.

44 le proteins having comparable differences in solvent exposure between their folded and unfolded state

45 Solvent exposure can be characterized by several measure

46 All 7 patients with solvent exposure carried the 2C19EM genotype, compared w

47 ull range of information on base-pairing and solvent exposure concerning the four more abundant ribon

48 eters such as backbone/Cu-loop dynamics, Cys solvent exposure, Cys-Cys distances, and cross-correlate

49 CA [cANCA] 3.9 [1.6-9.5]), high occupational solvent exposure during working lifetime (with PSV 2.7 [

50 rrounding the heme propionates leads to more solvent exposure for both propionate groups, which may a

51 ontexts were red shifted, indicating reduced solvent exposure for the fluorophore.

52 ha3 helix correlates with a higher degree of solvent exposure for this secondary structure element.

53 orted occupational activities with potential solvent exposure, furniture refinishing (OR = 9.73, 95 p

54 factors, where its side-chain is buried from solvent exposure in a hydrophobic cavity located beneath

55 ntiated connective tissue disease (UCTD) and solvent exposure in Michigan and Ohio.

56 with ANCA 4.9 [1.3-18.6]), high occupational solvent exposure in the index year (with PSV 3.4 [0.9-12

57 ing sites were chosen on the basis of a high solvent exposure in the native state and a small change

58 cular self-cleavage at Asp-193 evoked higher solvent exposure in the regions of the substrate-binding

59 Activities involving solvent exposure, including painting and use of solvents

60 Thus, insofar as solvent exposure is concerned, both the base- and the ac

61 redicts the effects on pKa values of various solvent exposures, large ionic strength variations, stro

62 ure, whereas the larger antagonists restrict solvent exposure largely through occlusion of solvent.

63 e results provide evidence that occupational solvent exposure may be associated with an increased ris

64 est accessible surface area, suggesting that solvent exposure may be relevant to the ability of the i

65 ta = 1.0) folate suggest that differences in solvent exposure may contribute to the fluorescence effi

66 Occupational solvent exposure may increase the risk of connective tis

67 arged residues, it was sometimes argued that solvent exposure meant that the high dielectric of the s

68 to examine the influence of bound ligands on solvent exposure of AChBP.

69 Solvent exposure of amino acid residues of proteins play

70 pattern correlates strongly with the average solvent exposure of amino acids in globular proteins, as

71 of Ca-ATPase-bound PLB, a decreased level of solvent exposure of ANSmal is observed, suggesting that

72 The increased solvent exposure of apolar surface area in the Ca(2+)-fr

73 egrees C) is reversible and characterized by solvent exposure of aromatic residues with concomitant d

74 rimental observations, notably the increased solvent exposure of buried residues in the breach region

75 lexibility, and correlations, as well as the solvent exposure of catalytic residues.

76 e changes cause a rotation of the B loop and solvent exposure of conserved phenylalanines, which are

77 on are highly correlated with the degrees of solvent exposure of corresponding positions in the arche

78 ve to Fe-EDTA-mediated cleavage, whereas the solvent exposure of D and E alpha-helices was decreased

79 of the core polymerase resulted in increased solvent exposure of DNA binding domains of sigma70 and i

80 The solvent exposure of each cysteine is ascertained by chem

81 distinguished from the "closed" form by the solvent exposure of F302, a direct T209-Mn2+ bond, and t

82 Bacterial MK proteins exhibit more solvent exposure of feedback inhibitor binding sites and

83 mide quenching is widely used to monitor the solvent exposure of fluorescent probes in vitro.

84 ce (helix H6) as well as the flexibility and solvent exposure of helix H11.

85 branes, the PPII helix may function to force solvent exposure of hydrophobic amino acid side chains i

86 is small and is indicative of a substantial solvent exposure of hydrophobic groups.

87 4 of the C-terminal domain experience strong solvent exposure of hydrophobic residues as well as part

88 This interaction prevents solvent exposure of hydrophobic residues on the surface

89 ied as hydrophobic or polar according to the solvent exposure of its generic side-chain.

90 Solvent exposure of loop C and its protection by ligand

91 rystallography revealed major differences in solvent exposure of MHC-bound peptide epitopes, suggesti

92 On synthetic liposomes, increased solvent exposure of MPER tryptophan residues and stable

93 gnificant structural changes that affect the solvent exposure of N-terminal region, and hence the red

94 The predicted solvent exposure of O6 at several subsites provides an e

95 e quenching experiments detected the partial solvent exposure of Pet aromatic amino acid residues at

96 ctural changes allow the protein to maintain solvent exposure of polar side chains and optimal burial

97 ive site, could result in an increase in the solvent exposure of Pro-1, raising its upper limit pK(a)

98 the larger methionine residue led to greater solvent exposure of residue 108 and heightened packing i

99 was associated with a selective increase in solvent exposure of residues 34 and 40, suggesting that

100 e accessibility method was used to probe the solvent exposure of single cysteine residues engineered

101 The reduced solvent exposure of TcTS catalytic cleft might be partia

102 is occupied by a ligand, the flexibility and solvent exposure of TcTS is significantly reduced.

103 t with decreased base stacking and increased solvent exposure of the 3-MI fluorescence probe.

104 opurine and FRET derivatives suggest greater solvent exposure of the 5'-AGGGTTA- segment in the inter

105 the reduced state possibly due to increased solvent exposure of the [3Fe-4S]0 cluster.

106 o map sites of ligand binding and changes in solvent exposure of the acetylcholine-binding protein fr

107 re of the EnXyn11A-FAX(3) complex shows that solvent exposure of the backbone xylose O2 and O3 groups

108 he sheet unfolds, increased fluctuations and solvent exposure of the beta-sheet amide groups are also

109 mature virions, consistent with the limited solvent exposure of the epitope.

110 tensively, and in a manner that will enhance solvent exposure of the FAD.

111 atic stacking interactions or to the greater solvent exposure of the flavin ring was not known.

112 MN hydroquinone rather than to the increased solvent exposure of the flavin.

113 , which deactivates catalysis, increased the solvent exposure of the globin domain-dimerization inter

114 two structures suggests that differences in solvent exposure of the heme and the electrostatic envir

115 R106L (DeltaE(m) = 158 mV vs NHE), increased solvent exposure of the heme as a result of the R106L su

116 the N- and C-terminal helices and subsequent solvent exposure of the hydrophobic, heme-containing cav

117 y of beta 2 compared to alpha beta is due to solvent exposure of the isoalloxazine ring in the beta 2

118 conformational flexibility and the extent of solvent exposure of the labile Asp residue.

119 This points to an increased solvent exposure of the NorC(sol) heme compared to in th

120 oss by the phenylalanine F12 band, signaling solvent exposure of the phenyl rings.

121 ng residues (P68, L69, Y166), increasing the solvent exposure of the polymorphic site.

122 g apoE3 NT mutant (L155W) revealed increased solvent exposure of the protein interior at pH values be

123 of the construct is consistent with partial solvent exposure of the tryptophan residues.

124 e chain vibrations, shows an increase in the solvent exposure of the tryptophan side chains as the te

125 und form and, in the apo form, determine the solvent exposure of the two Cys residues.

126 ellular membranes is linked to the degree of solvent exposure of their central and C-terminal hydroph

127 ain, complexed with mAb 64-3-7, demonstrates solvent exposure of these residues in the PR conformatio

128 g of sigma 70 to core polymerase reduced the solvent exposure of these residues.

129 ominance of this isomer is attributed to the solvent exposure of this portion of the hemin which stab

130 rylamide quenching suggest a higher level of solvent exposure of Trp-343 in the connector region of T

131 Reversal of the solvent exposure of Trp356 is also involved in cleft clo

132 e alpha domain leading to an increase in the solvent exposure of Trp48.

133 d dissociation was correlated with increased solvent exposure of tyrosine residues and subtle changes

134 lar dynamics simulations display alternating solvent exposure of Y671 in the closed and open states.

135 The higher solvent-exposure of hydrophobic residues in Abeta42 olig

136 beta2-alpha2 loop to beta turn increases the solvent-exposure of the hydrophobic stretch 169-YSNQNNF-

137 protein undergoes 93% of its total change in solvent exposure on going from the unfolded state to the

138 The nature of the preceding amino acid, the solvent exposure, or the participation in specific eleme

139 structures was found to better describe the solvent exposure over ASA, CN and RD in many application

140 a tyrosine residue(s) undergoes a change in solvent exposure over the pH range 6.55 to 8.19.

141 acrylamide quenching are consistent with the solvent exposure predicted for Trp28, which is shielded

142 local density term for each atom, mimicking solvent exposure preferences.

143 , indicating increased side-chain motion and solvent exposure relative to the spectra of the other Al

144 n correlation intensity corresponding to the solvent exposure/shielding alternation of the side chain

145 versus 71 patients with scleroderma without solvent exposure ("sporadic" disease) and 106 population

146 eased inter-beta-sheet distance and a higher solvent exposure than WT-alphaS fibrils, which is also i

147 tate on the reaction pathway, as measured by solvent exposure (the Tanford beta value) also moved wit

148 ence quantum yield that varies strongly with solvent exposure, thereby distinguishing particular DNA

149 Bound agonists restrict solvent exposure through loop closure, whereas the large

150 tophan oxidation correlates with the average solvent exposure time of tryptophan residues.

151 d the effects of local RNA structure on 2-AP solvent exposure to be distinguished from nearest neighb

152 Several case reports have linked solvent exposure to Parkinson disease (PD), but few stud

153 changing sites is consistent with a model of solvent exposure via a subglobal cooperative conformatio

154 Detailed information on solvent exposure was ascertained from 205 cases, diagnos

155 Occupational solvent exposure was categorized using self-reported job

156 Rather than emphasising solvent exposure with relatively extended sidechains, ro

157 d prevalence ratios were found for nonhexane solvent exposure, with a maximum of 1.31 (95% confidence

158 complementary information about mobility and solvent exposure yields a picture of the overall topolog