ライフサイエンスコーパス: heavy atom

1 high ligand efficiency (0.3-0.5 kcal/mol per heavy atom).

2 variant, within experimental error, with the heavy atom.

3 cies (LE) between 0.48 and 0.23 kcal/mol per heavy atom.

4 igand efficiencies from 0.442-0.637 kcal/mol/heavy atom.

5 te (13)C chemical shifts for carbons bearing heavy atoms.

6 rather than in the peptide plane defined by heavy atoms.

7 one atoms and 0.90 A (sigma = 0.122) for all heavy atoms.

8 pening of a cyclic hydrocarbon containing no heavy atoms.

9 0.41 A for backbone atoms and 0.88 A for all heavy atoms.

10 the backbone heavy atoms and 0.78 A for all heavy atoms.

11 the ability to access inner-shell states of heavy atoms.

12 A for the backbone atoms and 1.00 A for all heavy atoms.

13 A for backbone atoms and 1.42 +/- 0.16 A for heavy atoms.

14 for backbone heavy atoms and 0.83 A for all heavy atoms.

15 square deviation of 1.33 A over the backbone heavy atoms.

16 Calpha, C) atoms and 0.98 +/- 0.09 A for all heavy atoms.

17 0.30 A for backbone atoms and 0.71 A for all heavy atoms.

18 toms N, Calpha and C', and of 1.01 A for all heavy atoms.

19 for backbone heavy atoms and 1.02 A for all heavy atoms.

20 the backbone heavy atoms and 0.99 A for all heavy atoms.

21 ha, and C' atoms and 0.83 +/- 0.05 A for all heavy atoms.

22 backbone atoms and 1.10( +/- 0.08) A for all heavy atoms.

23 n was 0.75 A for backbone and 1.28 A for all heavy atoms.

24 uantum yields, which can be promoted by core heavy atoms.

25 ered aldol transition state containing eight heavy atoms.

26 A for backbone heavy atoms and 1.1 A for all heavy atoms.

27 lipophilicity with the addition of only two heavy atoms.

28 is the largest determined ab initio without heavy atoms.

29 entral atom that is being passed between two heavy atoms.

30 1,000,000-fold with the addition of only six heavy atoms.

31 nce homology and a low RMSD for the backbone heavy atoms (0.648 A) in the crystalline state, subtle,

32 The B-factors for most heavy atoms agree well with experiment (Pearson correlat

33 e X-ray scattering intensity arises from the heavy atoms, allowing direct extraction of pairwise dist

34 Spin density on the heavy atoms allows for increased isotropic and spin-orbi

35 These, in fact, often represent a heavy atom and its associated hydrogens (i.e. a united a

36 ned by taking into account the effect of the heavy atom and the rate of cage geminate radical pair re

37 (residues 13-80) is 0.37 A for the backbone heavy atoms and 0.78 A for all heavy atoms.

38 that exhibits an rmsd of 0.51 A for backbone heavy atoms and 0.83 A for all heavy atoms.

39 ues in the domain is 0.52 A for the backbone heavy atoms and 0.99 A for all heavy atoms.

40 verage rms deviations of 0.59 A for backbone heavy atoms and 1.02 A for all heavy atoms.

41 rmsd of the structure is 0.7 A for backbone heavy atoms and 1.1 A for all heavy atoms.

42 e mean structure was 0.82 A for the backbone heavy atoms and 1.3 A for all heavy atoms (residues 1-26

43 age rmsd of 0.35 and 0.90 A for the backbone heavy atoms and all heavy atoms of residues 14-72, respe

44 luding photo-crosslinkers, chemical handles, heavy atoms and post-translational modifications, and th

45 Atomic groups, which subsume a heavy-atom and its covalently attached hydrogen atoms in

46 ed structures are within 1.0-1.5 A (backbone heavy atoms) and 1.5-2.0 A (all heavy atoms) rms deviati

47 and potentials, including four larger (27-28 heavy atoms) and more conformationally flexible photochr

48 ms, 0.86 A (sigma = 0.12) for all associated heavy atoms, and 0.43 A (sigma = 0.17) for the heme grou

49 lectron basis set for iron, 6-311G for other heavy atoms, and 6-31G for hydrogen atoms, BPW91 and B3L

50 ncide with the bisectors of their respective heavy-atom angles.

51 simulation of protein folding, in which all heavy atoms are represented as interacting hard spheres.

52 en pairs of residues whose C(alpha) atoms or heavy atoms are within a cutoff distance.

53 Phosphorescence data are consistent with heavy-atom assisted intersystem crossing.

54 Placing heavy atoms at the alpha-position decreases conductance,

55 efined, with the backbone (N, Calpha, C) and heavy atom atomic rms distribution about the mean coordi

56 xperiments, adding the chemical shift of the heavy atom attached to the hydrogen ((13)C or (15)N nucl

57 values to the presence of a large number of heavy atoms (Au) in the framework and the formation of m

58 hPgn K3 was determined via NMR spectroscopy [heavy atom averaged rmsd = 0.35 +/- 0.07 A (backbone) an

59 A residue-based and a heavy atom-based statistical pair potential are develope

60 In the cases where heavy atom bond cleavage occurs concomitantly, the quest

61 onors, but not the lowest homolytic X-H (X = heavy atom) bond dissociation energies of the hydrogen-a

62 involve a combination of proton transfer and heavy-atom bonding changes are normally categorized by w

63 in that they are derived from only a single heavy atom change in the structure.

64 The examples were chosen to highlight single heavy atom changes that improve activity, rather than th

65 t of X-ray diffraction from an unoriented 18-heavy atom cluster derivative of a yeast RNA polymerase

66 of the method depends on the mobility of the heavy atom cluster on the particle, on the precision to

67 Heavy atom clusters may be introduced in a general way b

68 Heavy atom clusters should also allow selection of image

69 The particles will be labeled with multiple heavy atom clusters to permit the precise determination

70 deviation of 1.50 +/- 0.19 A taken over all heavy atoms, compared to 3.5 +/- 1.1 A for the ensemble

71 ynthesized TaIrGe compound made of all-metal heavy atom compound.

72 ide range of chemical probes and reagents; a heavy atom-containing amino acid for structural studies;

73 reactive configuration along the classical, heavy-atom coordinate, from which the hydrogen transfers

74 The backbone and heavy atom coordinates of structurally ordered amino aci

75 ay crystallography are commonly derived from heavy-atom coordinates by assuming idealized geometries.

76 dicts imino N-H vector orientations from the heavy-atom coordinates of the base pair.

77 The electron density maps and heavy atom data revealed the conformation of the nonheli

78 rhodopsin, but vary over a wide range after heavy atom derivatisation, with a between 101.5 A and 11

79 ght protein by combining them with the other heavy atom derivative data (multiple isomorphous replace

80 allographic studies through the binding of a heavy atom derivative, tungstate.

81 g using both the SeMet-labeled protein and a heavy atom derivative.

82 ith anomalous scattering (MIRAS) using three heavy atom derivatives and refined against X-ray diffrac

83 determined by isomorphous replacement using heavy-atom derivatives of both the wild-type protein and

84 arismortui by using phases derived from four heavy-atom derivatives, intercrystal density averaging a

85 ure was solved using standard techniques for heavy-atom derivatization of protein crystals.

86 tals, in analogy to the classic procedure of heavy-atom derivatization.

87 tional structure prediction and validated by heavy-atom derivatization.

88 d by tungsten cluster compounds bound in one heavy-atom-derivatized crystal.

89 d redox active amino acids, glycosylated and heavy atom derived amino acids in addition to those with

90 tions of distances between C(alpha) atoms or heavy atoms derived from a large set of protein crystal

91 From this initial discovery, a directed heavy atom design principle is demonstrated that will al

92 Similarly, species with lone pairs on heavy atoms dominate the potential energy surfaces of Al

93 The photodimerization exhibits a significant heavy atom effect and also is sensitive to selective que

94 fts and the change in the spin-orbit induced heavy atom effect of iodine compensate each other, and i

95 dependent correlation analysis and suggest a heavy atom effect of silver that rapidly depopulates an

96 The heavy atom effect strongly suggests a Trp location withi

97 te halogen bonding can be made to direct the heavy atom effect to produce surprisingly efficient soli

98 ystem crossing (ISC) is improved through the heavy atom effect, yet high quantum yields are achieved

99 sistent with an intersystem crossing-related heavy atom effect.

100 ate and suggests the occurrence of a mercury heavy atom effect.

101 R6WGR6 with poly(dABrdU) is diagnostic of a heavy atom effect.

102 The external heavy-atom effect of brominated host molecules leads to

103 be this to a resonant, remote intermolecular heavy-atom effect that greatly increases the inter-syste

104 pairs investigated, there were no observable heavy atom effects, from which it is concluded there is

105 -ZF, and reductions of D, but no significant heavy atom effects.

106 When iodoaniline residues were incorporated, heavy-atom effects led to enhanced (1)O2 production.

107 ggest that the enthalpic contribution to the heavy atom environmental reorganizations controlling the

108 e prepared which contained an intramolecular heavy atom for altering the fluorescence lifetimes to pr

109 0.12 A for backbone and 1.32 +/- 0.11 A for heavy atoms for amino acids 3-47.

110 f 0.25 A for the backbone and 0.61 A for all heavy atoms for residues Trp109-Gly263.

111 y verifies the X-ray diffraction study based heavy atoms formula, Au279S84, and establishes the molec

112 of the hydrogen positions relative to their heavy-atom frames considerably improves the fit of exper

113 indacene (BODIPY) dyes, recently proposed as heavy atom free photosensitizers for O(2)((1)Delta(g)) g

114 Heavy atom-free BODIPY-anthracene dyads (BADs) generate

115 gnificantly by the incorporation of a second heavy-atom group effecter.

116 mical structure for candidates with up to 30 heavy atoms has been reported previously by one of the a

117 The six-membered heavy atom heterocycles [Re(2)(CO)(8)(mu-SbPh(2))(mu-H)]

118 atize DNA or RNA by covalent attachment of a heavy atom (i.e., bromine at the C5 position of pyrimidi

119 tom in SECs might represent a non-functional heavy atom in an exotoxin group that has diverged from r

120 ientation of the planes associated with each heavy atom in interacting pairs.

121 en overlaid onto (1R,5R,9S)-(-)-10 using the heavy atoms in the morphan moiety as a common docking po

122 d phases accurate enough to locate the bound heavy atoms in three derivatives using difference Fourie

123 effective tool for determining the extent of heavy-atom incorporation in proteins.

124 Heavy-atom incorporation is an essential and often rate-

125 With no requirement for heavy-atom incorporation, such experiments provide an at

126 etermine protein structure-the ionization of heavy atoms increases the local radiation damage that is

127 enhanced indirectly by the incorporation of heavy atoms into nonspin-bearing sites, where they can c

128 anced by spin-orbit effects arising from the heavy-atom iodine substituent.

129 ded that the absorption cross-section of the heavy atom is considerably larger than those of its neig

130 ture (Q15-A42) is 0.71 +/- 0.12 A and of all heavy atoms is 1.07 +/- 0.08 A.

131 neurin by Mn2+ and Mg2+ was compared using a heavy atom isotope analogue of the substrate p-nitrophen

132 Heavy atom isotope effect and computational studies show

133 Heavy atom isotope effects are a valuable tool for probi

134 Heavy atom isotope effects at C-2, C-3, and the amino ni

135 erium isotope effects at C2 of aspartate and heavy atom isotope effects at C2, C3, and the amino grou

136 y labeled materials has precluded the use of heavy atom isotope effects to investigate mechanisms of

137 -2 of aspartate and of D(2)O on the observed heavy atom isotope effects were determined.

138 Heavy atom isotope effects were measured for Mg2+ activa

139 ally rate-limiting, consistent with previous heavy atom isotope studies (22).

140 Heavy-atom isotope effects for both leaving groups have

141 ed dihydrofolates allowed the measurement of heavy-atom isotope effects for the reaction catalyzed by

142 and S18A have been studied by measurement of heavy-atom isotope effects in the substrate.

143 lcineurin has been studied by measurement of heavy-atom isotope effects in the substrate.

144 The heavy-atom isotope effects were measured by isotope rati

145 were studied using steady state kinetics and heavy-atom isotope effects with the substrate p-nitrophe

146 Extensive heavy atom kinetic isotope effect and leaving group depe

147 the triester dimethyl pNPPT was probed using heavy atom kinetic isotope effects.

148 We now report the results of heavy-atom kinetic isotope effect measurements for the O

149 on catalyzed by AS-B at pH 8.0, substitution heavy atom labels in the side chain amide of the substra

150 ith that, we overcome the need of artificial heavy atom labels, the main obstacle to a broader applic

151 ollected on a protein incorporating specific heavy-atom labels in 65% aqueous sucrose buffer can dram

152 In addition to functioning as heavy atom markers in cross-sectional analysis by FIB an

153 The heavy-atom modification consisted of an intramolecular h

154 ion electrophoretic mobilities of the native heavy-atom-modified dyes were found to be very similar.

155 transfer undergoes several vibrations before heavy-atom motion completes the reaction.

156 the differing time scales for proton versus heavy-atom motion.

157 ansition state for hydride transfer from the heavy atom must have an even smaller volume, measured he

158 lity to now begin to predict essentially all heavy atom NMR hyperfine shifts in paramagnetic metallop

159 n residues correlate with both the number of heavy atom (nonproton) gamma-substituents and with gauch

160 d in an antiparallel alignment, with the nth heavy atom of one side chain in registration with the (o

161 chain in registration with the (omega+2-n)th heavy atom of two adjacent chains ((omega <--> 2) packin

162 0.38 A for backbone atoms and 0.94 A for all heavy atoms of ordered residues 5-41 and 50-69.

163 Superposition of backbone heavy atoms of ordered residues relative to mean atom po

164 0.90 A for the backbone heavy atoms and all heavy atoms of residues 14-72, respectively.

165 lature from eight-membered cycloalkanes, the heavy atoms of the low-energy transition states are in c

166 re for the backbone atoms, and 1.2 A for all heavy-atoms of the dimeric core (helices 1 and 2) and th

167 The rms deviation between the heavy-atoms of the ten lowest-energy structures is 1.24

168 Although single heavy atoms on surfaces or supporting films have been vi

169 6 +/- 0.17 A, respectively, for backbone and heavy atom overlays of residues 1-34.

170 per molecule is 4, and the average number of heavy atoms per side chain is 2.

171 The nature of the heavy atom perturbation, however, was found to be differ

172 p-probe method used p-dichlorobenzene as the heavy atom perturber, whereas the steady-state method us

173 Here, synchrotron XRD data provide all heavy-atom positions in (+)-catechin 4.5-hydrate and est

174 A final improvement to heavy-atom positions is provided by a geometry optimizat

175 tions of the crystallographically determined heavy-atom positions or ad hoc adjustments of the intrin

176 d in the presence and absence of an external heavy atom probe.

177 site-specifically labeling RNA with pairs of heavy atom probes, and precisely measuring the distribut

178 l in cases where protein derivatization with heavy atoms proves to be problematic or synchrotron faci

179 lar system occurs predominantly locally on a heavy atom (provided that the absorption cross-section o

180 fills the core holes that are created in the heavy atom, providing further targets for inner-shell io

181 structures with high accuracy (0.6-2.0 A all-heavy-atom r.m.s. deviation) in 18 cases.

182 s in stable radical chemistry have afforded "heavy atom" radicals, neutral open-shell (S = 1/2) molec

183 ourea has different chemical properties than heavy-atom reagents and halide ions and provides a conve

184 perpendicular to the membrane plane using a heavy atom refinement algorithm.

185 ordinates combined with multiple isomorphous heavy atom replacement.

186 two virtual atom representations and one all-heavy atom representation.

187 r the backbone heavy atoms and 1.3 A for all heavy atoms (residues 1-26, 37-60).

188 r the backbone (N, C', and C(alpha)) and all heavy atoms (residues 4-224) of 0.69 +/- 0.09 and 1.04 +

189 These pseudo-4D heavy-atom resolved [(1)H, (1)H]-NOESY experiments conta

190 d (0.66 and 0.97 D rmsd for backbone and all heavy atoms, respectively) with a compact hydrophobic co

191 and 0.90 angstroms for the backbone and all heavy atoms, respectively, for residues 2-83.

192 +/- 0.13) angstroms for the backbone and all heavy atoms, respectively, of all residues except 28 to

193 92 +/- 0.20 A for the backbone atoms and all heavy atoms, respectively, of all residues except Ala32-

194 .07 and 0.84 +/- 0.11 A for the backbone and heavy atoms, respectively.

195 11 +/- 0.19 A for the backbone atoms and all heavy atoms, respectively.

196 .31 and 1.35 +/- 0.34 A for the backbone and heavy atoms, respectively.

197 98 +/- 0.23 A for the backbone atoms and all heavy atoms, respectively.

198 inhibitor fosimdomycin to Mn(2+)-DXR (ligand heavy atom rms deviation = 0.90 A) and is poised to inte

199 to represent the structure had backbone and heavy atom rms deviations of 0.46 +/- 0.11 and 1.02 +/-

200 A (backbone heavy atoms) and 1.5-2.0 A (all heavy atoms) rms deviations from reported x-ray and/or N

201 the free DNA structure and the 2:1 complex (heavy atom RMSD 1.55 A) reveal that these sequence-depen

202 CHA was solved via NMR spectroscopy (protein heavy atom RMSD approximately 0.93 +/- 0.12 A).

203 parameter, consistent with a higher backbone heavy atom RMSD of approximately 1.22 A (vs 0.84 A overa

204 The average backbone and heavy atom rmsd values of the 20 structures (residues 7-

205 The average backbone and heavy atom rmsd values of the 20 structures (residues 9-

206 The backbone heavy-atom RMSD for residues L14 through M21 is 0.09 +/-

207 ugh M21 is 0.09 +/- 0.12 A, and the backbone heavy-atom RMSD for the whole peptide is 0.96 +/- 2.45 A

208 xperimentally determined structures with all-heavy-atom RMSDs ranging from 2.4 to 6.5 A.

209 e root mean square deviation of 0.46 A and a heavy atom root mean square deviation of 0.93 A.

210 lation stays true to the crystal form with a heavy atom root mean-squared deviation of 2 A.

211 reproduce X-ray ligand positions within 2.0A heavy atom root-mean-square deviation.

212 test proteins, decoys with 1.7- to 4.0-A all-heavy-atom root mean-square deviations emerge as those w

213 The heavy atom scatterer peak was now prominent in the FT an

214 at 2.7 A was suggestive of the presence of a heavy atom scatterer such as Cu.

215 different from that via ISC originating from heavy atom spin-orbit coupling.

216 the excited vibrational bending (01(1)0) and heavy atom stretching (100) modes were measured.

217 To test this hypothesis, heavy atom substituted DBTOs were prepared and photolyze

218 orogen-activating protein (FAP) that binds a heavy atom-substituted fluorogenic dye, forming an 'on-d

219 Optical spectroscopy reveals that heavy atom substitution leads to a red-shift in the low-

220 The effects of tacticity, heavy atom substitution on the main chain, and chain hel

221 Heavy-atom substitution alone increases phosphorescence

222 nt-free lactide polymerization combined with heavy-atom substitution.

223 small polyatomic molecules that contain one heavy atom to ultra-intense (with intensities approachin

224 including adding a limited number of missing heavy atoms to biomolecular structures, estimating titra

225 A for backbone atoms and 0.71 +/- 0.07 A for heavy atoms to the mean structure.

226 erium isotope effect (CH3OD), this motion of heavy atoms transforms the reverse charge transfer from

227 f substituents on a possible contribution of heavy atom tunneling to the reaction mechanism is also d

228 on to recent experimental findings that show heavy-atom tunneling at moderate temperatures.

229 support the recently predicted importance of heavy-atom tunneling in cyclopropylcarbinyl ring-opening

230 d out for 13 reactions, to test the scope of heavy-atom tunneling in organic chemistry, and to check

231 ntal test of the theoretical prediction that heavy-atom tunneling is involved in the degenerate Cope

232 In this way, we discovered the heavy-atom tunneling reaction involving spontaneous ring

233 ple computational test for the likelihood of heavy-atom tunneling using standard quantum-chemical inf

234 nce, the results are interpreted in terms of heavy-atom tunneling.

235 en-1,5-diyne were carried out to investigate heavy-atom tunneling.

236 for predicting transmission coefficients in heavy-atom tunnelling.

237 d efficiencies of 0.29-0.54 kcal mol(-1) per heavy atom were achieved.

238 ed with the transfer of chlorine between two heavy atoms, whereas in the presence of low H3O(+) and C

239 was 1.01 +/- 0.13 A (1.52 +/- 0.12 A for all heavy atoms), which improved to 0.49 +/- 0.05 A (1.19 +/

240 mic clusters to mimic the chemistry of these heavy atoms, which will be of great importance in design

241 y enhanced compared to that of an individual heavy atom with the same absorption cross-section.

242 re deviations (RMSD) for all of the backbone heavy atoms with respect to the native structure of 3.35