ライフサイエンスコーパス: absorption maximum

1 an unexpected light-induced red-shift of the absorption maximum.

2 he differences in excited-state lifetime and absorption maximum.

3 harged carboxylates causes red shifts of the absorption maximum.

4 t wavelengths significantly shorter than its absorption maximum.

5 nt in the QD excitation near the J-aggregate absorption maximum.

6 athochromic shifts of the longest wavelength absorption maximum.

7 re involved in fine-tuning the chromophore's absorption maximum.

8 ted acyl group, and a large red shift in the absorption maximum.

9 395 nm and 460 nm) on either side of the PYP absorption maximum (446 nm) were undertaken using 100-fs

10 Its absorption maximum, 474 nm, is greatly red shifted compa

11 e found that the resulting enzyme is a blue (absorption maximum 590 nm) complex containing MnxE, MnxF

12 crograms of phosphorescence probe (Green 2W; absorption maximum 636 nm) was injected into the tail ve

13 A systematic shift in the absorption maximum (637-655 nm for the free base chlorin

14 le chromophore can be manipulated to have an absorption maximum across such an extended spectral regi

15 isible light-absorbing pigment with a 534 nm absorption maximum and approximately 100 nm half-bandwid

16 The absorption maximum and quantum yield for the decaging of

17 The position of the absorption maximum and shape of the band is consistent w

18 ve cytoplasmic transducer protein shifts the absorption maximum and strongly decreases the rate of da

19 lectron's radius of gyration and its optical absorption maximum, and extrapolating to the bulk limit

20 O-like in its C-C stretch bands, but has an absorption maximum apparently close to that of unphotoly

21 he nature of the assay product, which has an absorption maximum around 470 nm, had not been determine

22 light inactivation and a red-shifted visible absorption maximum as compared with the more extensively

23 affording another bathochromic shift with an absorption maximum at 1095 nm and a fluorescence peak at

24 Copper-containing CBCs showed a broad absorption maximum at 245 nm.

25 oduce high molecular weight material with an absorption maximum at 260 nm.

26 redshift of its absorption spectrum from an absorption maximum at 267 nm in thymidine to 363 nm in 2

27 pectra show the covalent intermediate has an absorption maximum at 310 nm.

28 The probe exhibited absorption maximum at 374nm and emission maximum at 467n

29 of oxidized C. tepidum Rd exhibited a unique absorption maximum at 385 nm and a shoulder at 420 nm.

30 In the presence of BH4, eNOS has an absorption maximum at 400 nm that shifts to 395 nm when

31 eveal the characteristic low-spin FeIII heme absorption maximum at 418 nm.

32 teinylglycine [NO2ZGly(S-NBD)CysGly] with an absorption maximum at 423 nm is readily hydrolyzed by an

33 mperature, the X. laevis violet opsin has an absorption maximum at 426 nm when generated with 11-cis-

34 intermediate has a significantly red-shifted absorption maximum at 440 nm, suggesting that the retiny

35 roteins bind heme and exhibit the ferrous-CO absorption maximum at 444 nm characteristic of thiolate

36 rmation of an Fe(II)-CO complex with a Soret absorption maximum at 448.5 nm, which collapses (at 0.24

37 re P450s, i.e. they have a "pigment" with an absorption maximum at 450 nm.

38 e violet cone opsin generated at 45 K has an absorption maximum at 450 nm.

39 The bound FAD displayed an absorption maximum at 464 nm with an extinction coeffici

40 acetylene-iron spectral intermediate with an absorption maximum at 485 nm.

41 nitial (or spectrally similar) state with an absorption maximum at 501 nm upon illumination with 380-

42 The AMTr-AuNPs show the absorption maximum at 520 nm and emission maximum at 759

43 pectrum to yield a 28% greater intensity, an absorption maximum at 520 nm, and distinct shoulders at

44 The visible spectrum exhibited an absorption maximum at 550 nm with a shoulder at 635 nm.

45 lation, forms a light-sensitive pigment with absorption maximum at 560 nm upon reconstitution with 11

46 Concentrated samples of native PALcc have an absorption maximum at 560 nm, suggestive of a phenolate-

47 nactive blue form of the enzyme with a broad absorption maximum at 650 nm.

48 arotenoid cation radical is formed having an absorption maximum at 898 nm, an 85 nm blue shift relati

49 m Thiorhodovibrio strain 970 exhibits an LH1 absorption maximum at 960 nm, the most red-shifted absor

50 lar J-type exciton coupling, resulting in an absorption maximum at 961 nm and a fluorescence peak at

51 prepared zinc arylsulfanyl TPyzPzs showed an absorption maximum at a Q-band over 650 nm, fluorescence

52 1-10, the latter had an additional, uncommon absorption maximum at approx. 585 nm at slightly acidic

53 ark and the batho intermediates) that has as absorption maximum at approximately 470 nm, and thermall

54 The generated AuNPs@DD has an absorption maximum at approximately 518 nm.

55 urther decrease in pH from 2 to 0 shifts the absorption maximum back to 575 nm when HCl is used (acid

56 components were used to predict their plasma absorption maximum, based on molecular mass and lipophil

57 date, with Chl f having the most red-shifted absorption maximum because of a C2(1)-formyl group subst

58 cular framework shows that the excited-state absorption maximum can be extensively modulated [lambdam

59 of the solvent on the position of the UV-vis absorption maximum, can be determined via a linear Hamme

60 d to account for the 30 nm blue shift of its absorption maximum compared to that of the green pigment

61 The absorption maximum for the encapsulated Reichardt's dye

62 The value of the electronic absorption maximum for the HAV 3C (C24S) acyl enzyme and

63 The predicted absorption maximum for the model structures for 13, 14,

64 ring and consequently to a red shift of its absorption maximum from 446 nm to 457 and 458 nm in the

65 e Glu46Gln mutation shifted the ground state absorption maximum from 446 to 462 nm, indicating that t

66 W265Y, A292S, A295S, and A299C) shifted the absorption maximum from 500 to 438 nm, accounting for 2,

67 ge of pH from 6.5 to 2 causes a shift of the absorption maximum from 568 to 600 nm (acid blue bR) and

68 ff base, resulting in a shift of the optical absorption maximum from 600 nm to 400 nm.

69 the removal of this dipolar field shifts the absorption maximum from blue to green.

70 the S65G and S72A mutations which shift the absorption maximum from the 395 nm of wild-type GFP clos

71 viscosity coordinating solvents, the initial absorption maximum further red shifts between 2 and 10 p

72 Binding of lutein (absorption maximum in hexane at 454 nm) to the apoprotei

73 zation, display a similar longest wavelength absorption maximum in solution.

74 lower frequency upon deprotonation, and the absorption maximum in the UV-visible spectrum shifts to

75 ntal spectrum of the blue form in DsRed (the absorption maximum is 408 nm or 3.04 eV) and mTagBFP (40

76 ong-wave subfamily of cone pigments, but its absorption maximum is 508 nm, similar to that of the rho

77 ted state of 474 nm, while the metarhodopsin absorption maximum is 572 nm.

78 e flavin domain and a species with a similar absorption maximum is also seen during reduction of the

79 Under aerobic conditions, a second absorption maximum is observed with lambda(max) = 366 nm

80 s retinal as does the N state of BR, but its absorption maximum is red-shifted relative to PR (like t

81 The computed absorption maximum is red-shifted when compared to the g

82 ing two Se atoms for S gave a shorter band I absorption maximum (lambda(max) of 695 nm) and a smaller

83 Unbound TO-PRO-3 has an absorption maximum (lambda(max)) of 632 nm, while the bo

84 in the bandwidth closest to the indicator's absorption maximum (lambdamax) at pHs above the indicato

85 trix-isolated 1 at lambda = 222 nm (near its absorption maximum) led to the corresponding 2H-azirine

86 This absorption maximum lies between that of unbound retinal

87 487 nm absorption maximum to a species with absorption maximum near 350 nm (M) followed by a species

88 ht sensitivity of SCN-projecting RGCs has an absorption maximum near 484 nm.

89 e among the archaeal rhodopsins in having an absorption maximum near 500 nm, blue shifted roughly 70

90 The data show that CSRA has an absorption maximum near 510 nm and mediates a fast photo

91 ual high-potential haem c with a red-shifted absorption maximum, not unlike that of certain eukaryoti

92 At room temperature, mouse UV opsin has an absorption maximum of 357 nm, while at 70 K, the pigment

93 ation, the blue pigment exhibits an absolute absorption maximum of 414 nm.

94 nm when generated with 11-cis-retinal and an absorption maximum of 415 nm when generated with 9-cis-r

95 obenzene-3, 4'-disulfonic acid, which has an absorption maximum of 489 nm and an extinction coefficie

96 The absorption maximum of 8-nitroxanthine shifts from 380 to

97 kene moieties result in a longest-wavelength absorption maximum of about 350 nm.

98 sin, a retinal-protein intermediate, with an absorption maximum of about 430 nm, has been identified.

99 the fluorescent drug-tubulin complex at the absorption maximum of anthranilate, yields a covalent ad

100 The absorption maximum of blue proteorhodopsin (BPR) is the

101 In the low density fraction, the absorption maximum of BR was blue-shifted by 2 to 4 nm r

102 strate that the longitudinal surface plasmon absorption maximum of GNRs is correlated with the effect

103 btained at a wavelength corresponding to the absorption maximum of liquid water of about 2.94 mum.

104 nd CH vibrational bands of the alcohols, the absorption maximum of Reichardt's dye redshifted by up t

105 itted fluorescence of azido-ATP-EDANS at the absorption maximum of S135C-EMA and a corresponding 50%

106 ively causes (1) a bathochromic shift in the absorption maximum of the B band (405 to 426 nm) and (2)

107 , progressively causes (1) a redshift in the absorption maximum of the B band (405-436 nm) and the Q(

108 erved for the GFP emission, excited near the absorption maximum of the BFP, is very low due to depola

109 as about equal to the difference between the absorption maximum of the bullfrog and newt pigments, 44

110 to the extreme red shift (ca. 80 nm) of the absorption maximum of the carotenoid bound by the CCP2 d

111 We also found that at high pH, the absorption maximum of the chloride-free pigment shifts f

112 Purified Rh1-1D4 visual pigment has an absorption maximum of the dark-adapted state of 474 nm,

113 the complex to protein causes a shift in the absorption maximum of the dye-metal complex from 450 to

114 The first determination of the absolute absorption maximum of the human blue cone visual pigment

115 The 32 nm shift of the absorption maximum of the multiple seven-residue mutant

116 urface plasmon resonance wavelength with the absorption maximum of the NIR dye to maximize the plasmo

117 e accompanied by a hypsochromic shift of the absorption maximum of the photoinduced form, whereas no

118 The short wavelength of the absorption maximum of the photoproduct indicates that it

119 the host protein, enabled regulation of the absorption maximum of the pigment in the range of 425 to

120 hat observed for the analogous excited-state absorption maximum of the PZnE-EPZn benchmark; these dat

121 In contrast, the absorption maximum of the red-shifted beta-carotene was

122 The residue substitutions did not alter the absorption maximum of the signal, ruling out contributio

123 Chloride ions do not affect the absorption maximum of the violet opsin.

124 gradual blue-shift in the wavelength of the absorption maximum of their visual pigments with increas

125 In the case of the basic form of E113Q, the absorption maximum of this intermediate was at 408 nm.

126 n is observed for 1-7 with the lowest-energy absorption maximum (Q band) varying little as a function

127 or the 70- to 80-nanometer blue shift of its absorption maximum relative to those of haloarchaeal tra

128 On oxidation with K3Fe(CN)6, the absorption maximum shifted to 540 nm and a new shoulder

129 The initial absorption maximum shifts to longer wavelengths in coord

130 ChR variants with a red-shifted absorption maximum, such as the modified Volvox carteri

131 and broader and with lower extinction at the absorption maximum than either the human blue or salaman

132 Consistent with the red-shift of the absorption maximum, the chloride bound near the Schiff b

133 hway from the unphotolyzed state with 487 nm absorption maximum to a species with absorption maximum

134 itterions of amino acids in DMSO, and its UV absorption maximum undergoes a significant red shift in

135 The absorption maximum undergoes an analogous shift from 400

136 fraction contained BR in a lattice form: its absorption maximum was blue-shifted by < or = 4 nm relat

137 ed hyperchromic shift by up to +50.5% at the absorption maximum was observed at pH 4.6.

138 ansition in the i-motif form relative to its absorption maximum, which agrees with the experimental a

139 s in a significantly smaller redshift in the absorption maximum, which depends sensitively on the pos

140 cence emission and a 45 nm blue shift of the absorption maximum with an increase in the pH from 5 to