ライフサイエンスコーパス: I band

1 and peptide groups associated with the amide I band.

2 hich resulted in a large change in the amide I band.

3 g domain from the distal region of the titin I-band.

4 domain from the proximal region of the titin I-band.

5 extra series compliance is introduced in the I-band.

6 omains which were previously assigned to the I-band.

7 localize to the M-line and a portion of the I-band.

8 0 nm (up to three regulatory units) into the I-band.

9 rational circular dichroism of the two amide I bands.

10 gularly 50% of the proportion of stalks with i bands.

11 a approximately 40 cm(-1) shift in the amide I' band.

12 ochondrial localization to actin-rich muscle I-bands.

13 ity important for localizing mitochondria to I-bands.

14 sembly of A- and M-bands, but not Z-disks or I-bands.

15 Amide I bands (1,700-1,600 cm(-1)) are the most prominent and

16 of absorbance intensity mainly in the amide I band (1600-1700 cm(-1)) as well as in the amide II and

17 ur via anchor protein diffusive motion, that is, band 3 and glycophorin, through the membrane.

18 ments producing myofibrils with well defined I bands, A bands, and H zones.

19 Genetic deletion of the I-band-A-band junction (IAjxn) in titin increases strain

20 ibronectin type 3 domains that comprises the I-band/A-band (IA) junction and obtained a viable mouse

21 ice-matched GaN substrate, possessing a type-I band alignment, exhibits strong substrate-induced inte

22 mined that KLHL40 localizes to the sarcomere I band and A band and binds to nebulin (NEB), a protein

23 t (66%), confirmed by narrowing of the amide I band and the profile maximum shifting to 1667 cm(-1).

24 spectral features studied included the amide I' band and the side-chain absorbances for aspartate res

25 ional boundary lies between the myofibrillar I-band and intercalated disc thin filaments, identifiabl

26 ng, both of these antibodies localize to the I-band and may extend into the outer edge of the A-band

27 Extraction of TnC-reduced I-band and overlap Ca in rigor fibers at pCa 5.6 to the

28 threshold for activation, Ca was the same in I-band and overlap regions.

29 d impaired function with specific changes in I-band and Z-disk proteins by 6 months of age.

30 ctromechanical coupling, consistent H-zones, I-bands, and evidence for T-tubules and M-bands.

31 myotubes were incorporated selectively into I-band approximately 1.0-micrometer F-alpha-actin-contai

32 uorescent dye, and a small volume within the I-band ( approximately 10(-16) L), containing on average

33 asp localizes to the Z-disc edges to control I-band architecture and also localizes at the A-band, wh

34 of TTN cause DCM, whereas truncations in the I band are better tolerated.

35 main boundaries, the properties of the titin I-band are essentially "the sum of its parts".

36 ational frequency inhomogeneity of the amide-I band arises from fluctuations of the instantaneous nor

37 The two observed amide I bands at 1615 cm(-1) and 1656 cm(-1) are shown to aris

38 egreesC, as shown by the appearance of amide I bands at 1617 and 1682 cm-1.

39 aments, was significantly higher than in the I-band at all pCa levels tested between 6.9 and 4.8, but

40 eaction-induced spectra also exhibited amide I bands, at 1661 and 1652 cm(-1).

41 Amide I band attenuated total reflection/Fourier transformed i

42 ing from the Z-line, whereas the rest of the I-band became devoid of thin filaments, exposing titin.

43 titin antibodies show localization to muscle I-bands beginning at the L2-L3 larval stages and this pa

44 Actin is found in normal-appearing I-bands, but with abnormal accumulations near muscle cel

45 overlap between water and the protein Amide I band centered at 1650 cm(-1).

46 It is found that although the amide I band changes its frequency on a time scale of <100 ns,

47 I-band compliance during rigor induction was 35% of sarc

48 rations in the relative intensities of Amide I band constituents are interpreted using a semiempirica

49 urements were strongly correlated with amide I band data which indicated that the decrease in the LCS

50 respective intensity ratios of the two amide I bands depend on the excitonic coupling between the ami

51 FTIR studies of the amide I band did not show a single prevailing secondary struct

52 ied the changes in the (12)C and (13)C amide I' band due to label position.

53 ured every 50 ms from the center half of the I-band during 60 s of rigor, relaxation and contraction

54 We also determined compliance of the I-band during rigor.

55 des that can exceed a factor of three in the I-band flux.

56 proteins and their fragments and (13)C-amide I' bands for multiple isotopologues of each protein.

57 bserved a significant downshift of the amide I band frequency of Abeta peptides in Dementia Alzheimer

58 ing the change in the frequency of the amide I band from 1667 to 1651 cm-1 and the shift in the frequ

59 N isotope labeled G-CSF to resolve its amide I' band from that of the receptor in the IR spectrum of

60 egments (IS and OS, histology) separates the IS band from retinal pigment epithelium.

61 We show that adjacent domains in the titin I-band have very different kinetic properties which, in

62 this structure as well as that of the nearby I band in a normal, unstimulated mammalian skeletal musc

63 ansmission measurements of the protein amide I band in aqueous solution at large optical paths.

64 e located at different sarcomeric locations, I band in the IFM and A band in synchronous muscles.

65 s of total calcium along the length of A and I bands in skinned frog semitendinosus muscles using ele

66 states of tri-alanine by analyzing the amide I bands in the respective IR and isotropic Raman spectra

67 ties of five immunoglobulin domains from the I-band in three different contexts; firstly as isolated

68 ote mitochondrial localization to actin-rich I-bands in body wall muscle.

69 (2) Ce titins are not localized to I-bands in embryonic or L1 larval muscle.

70 cular beta-sheet, deconvolution of the amide I band indicates that formation of hexamers stabilizes b

71 Measurements of surface pressure, Amide I band intensities, and LPS acyl chain conformational or

72 her narrowing of a beta-sheet-specific amide I band is observed on reorganization of insulin in a cro

73 The amide I band is very sensitive to peptide secondary structure,

74 The amide I' band is exquisitely sensitive to changes in protein s

75 tion of titin epitopes at the thick-filament/I-band junction.

76 t, the power of the correlated oxygen signal is band limited from approximately 0.01 Hz to 0.4 Hz wit

77 Analysis of amide I band line shapes through Fourier deconvolution and non

78 The amide I band maximum above or below the decisive marker freque

79 However, previous SMD studies of titin I-band modules have been restricted to I27, the only str

80 tions in the assembly and maintenance of I-Z-I bands, MYC- and GFP- tagged nebulin fragments were exp

81 d in an irreversible alteration in the amide I band noted in the infrared spectra for both purified t

82 uction in the intensity of a prominent amide I band observed for SRII indicates that its structural c

83 ting is used to characterize the Raman amide I band of alpha-synuclein, phosvitin, alpha-casein, beta

84 e-fitting analysis were applied to the amide I band of FTIR spectra for detail analysis of secondary

85 Raman amide I band resembles the Raman amide I band of ionized polyglutamate and polylysine, peptides

86 Infrared (IR) spectroscopy of the amide I band of polypeptides can be used to probe both seconda

87 semble of exciton Hamiltonians for the amide-I band of the folded and unfolded states of a helical be

88 citonic coupling model to simulate the amide I band of the FTIR, vibrational circular dichroism, and

89 ts in tandem immunoglobulin domains from the I band of titin under native conditions.

90 ing between the conformation-sensitive amide I bands of alpha-crystallin and unlabeled substrate prot

91 The amide I bands of specifically labeled helices should vary syst

92 , as indicated in the downshift of the amide I' band of both apo-CaM and Ca(2+)-CaM, and a modificati

93 perature jump, obtained by probing the amide I' band of the peptide backbone, exhibit nonexponential

94 ng sharp peak (1675 cm(-1)) within the amide I' band of the spectral region.

95 In addition, we find that the amide I' band of this beta-peptide exhibits a sharp feature at

96 STARS binds to the I-band of the sarcomere and to actin filaments in transf

97 he spring-like (PEVK) domain of titin at the I-band of the sarcomere.

98 a subset of circRNAs that originate from the I-band of the titin gene.

99 Analysis of the complex I band on an SDS gel showed a major peak of radioactivit

100 The elastic I-band part of muscle protein titin contains two tandem

101 A small region in the I-band part of the molecule, which probably corresponds

102 ately 100 nm long) tryptic fragment from the I-band part of titin that is extensible in situ.

103 tour length from the physiologically elastic I-band part.

104 pulling experimental data for I91 from titin I-band (PDB ID: 1TIT) and ubiquitin (PDB ID: 1UBQ).

105 stinct types of spring-like behaviour of the I-band portion of the molecule.

106 nfluences of excitonic coupling on the amide I band profile in the isotropic and anisotropic Raman, F

107 The amide I band profile of the IR, isotropic and anisotropic Rama

108 residue was achieved by analyzing the amide I band profile of the respective polarized visible Raman

109 residues was achieved by analyzing the amide I' band profile in the respective polarized visible Rama

110 Analysis of the Raman amide I band profiles of the different alpha-synuclein oligome

111 duction of the experimentally observed amide I' band profiles.

112 n structure estimation technique using amide I band Raman spectroscopy.

113 ircular dichroism (VCD) couplet in the amide I' band region that is nearly 2 orders of magnitude larg

114 ent structural elements within their central I-band region are expressed in human myocardium.

115 The majority of titin's I-band region functions as a molecular spring.

116 cardiac triadin is primarily confined to the I-band region of cardiac myocytes, where the junctional

117 r origin of the in vivo extensibility of the I-band region of cardiac titin.

118 eins was increased in the nucleus and at the I-band region of myofibrils, while DARP staining also in

119 The I-band region of the giant muscle protein titin contains

120 This force is generated by the extensible I-band region of the molecule, which is constructed of t

121 e properties of the unique N2B sequence, the I-band region of the N2B cardiac titin isoform functions

122 In the I-band region of the sarcomere, where titin extends and

123 circRNAs originated from the RBM20-regulated I-band region of the titin transcript.

124 The I-band region of titin contains tandem Ig segments (cons

125 The I-band region of titin is responsible for passive elasti

126 We address this question for the I-band region of titin, which is of particular biologica

127 This force arises from titin's extensible I-band region, which consists mainly of three segment ty

128 Titin's force arises from its extensible I-band region, which consists of two main segment types:

129 Titin's force is generated by its I-band region, which includes the cardiac-specific N2B e

130 elastic and extensibility properties in its I-band region, which is largely composed of a PEVK regio

131 Titin's force is derived from its extensible I-band region, which, in the cardiac isoform, comprises

132 t 40 immunoglobulin-like (Ig) domains in its I-band region.

133 ut, surprisingly, not of the NH2-terminal or I-band regions of titin, the Z-lines, or the thin filame

134 y feature of the alpha-synuclein Raman amide I band resembles the Raman amide I band of ionized polyg

135 he carbonyl groups associated with the amide I band results in a strong chiral contribution to the op

136 ion measurements of cdS1 bound to individual I-bands revealed that the orientation depended on the co

137 Infrared spectroscopy of the amide I band reveals that the proteins retain secondary struct

138 The analysis of the amide-I' band reveals another major component at 1650 cm-1 ass

139 Extension of the I-band segment of titin gives rise to a force that under

140 Extension of the I-band segment of titin gives rise to part of the diasto

141 The I-band segment of titin is considered to function as a m

142 We found that only a small region of the I-band segment of titin is elastic; its contour length i

143 eries of differential splicing events in the I-band segment of titin leading to the so-called N2A and

144 In the sarcomere, the elastic I-band segment of titin may interact with the thin filam

145 al muscle indicate that it is not the entire I-band segment of titin that behaves as a spring; some s

146 which is only approximately 40% of the total I-band segment of titin.

147 anomeric (H1) region of the 1H NMR spectrum is band-selected in the F1 dimension.

148 ructure selectivity of the distinctive amide I' band shapes that arise in isotopically edited spectra

149 ry proof-of-concept study indicated an amide I band shift below the marker band already in patients w

150 ermal denaturation of the peptide, the amide-I band shifts to higher frequency because the increase i

151 The Fourier transform infrared (FTIR) amide I band shows that antiparallel beta-sheet structure incr

152 On gentle slopes the typical pattern form is bands (stripes), oriented parallel to the contours, a

153 the giant protein titin span the A-bands and I-bands that make up striated muscle.

154 ent domains may be a general property of the I-band thereby preventing misfolding events on muscle re

155 in was found to be high, relative to that of I-band titin ( approximately 40-fold higher) but low, re

156 In the I-band titin extends as the sarcomere is stretched, deve

157 emperature demonstrate that titin-II and the I-band titin fragment experience a similar denaturation

158 ee endogenous MARP proteins co-localize with I-band titin N2A epitopes in adult heart muscle tissues.

159 ct pair formation, the response of the amide I band to the nature and concentration of salt was monit

160 In SM, Ca(2+) shifts the amide I' band to frequencies lower than those in dehydrated sa

161 osin filaments, can redistribute through the I-band to their anchoring sites in the tetragonal Z-band

162 resent at all temperatures, shifts the amide-I band toward lower frequency compared with the unsolvat

163 led that the elastic segment of titin in the I band was missing from the sarcomere.

164 M-bands and A-bands, but not Z-disks or I-bands, were disrupted when the synthesis of obscurin w

165 ntially by stabilizing thin filaments in the I-band, where nebulin and thin filaments coalign.

166 The sensor detected the amide I band, which reflects the overall secondary structure d

167 determined by the highly reproducible amide-I band widths, linking aggregation propensity and fibril

168 , protein loaded at pH 4 has a broader amide I band with more intensity in the >1680 cm(-1) region.

169 oreover, solvent exposed residues have amide I bands with >20 cm(-1) line width.

170 A similar set of amide I bands, with frequencies of 1675 and 1651 cm(-1), was o