ライフサイエンスコーパス: I band

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

2 and peptide groups associated with 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 ring to adapt its length to the width of the I-band.

8 protein located in the sarcomeric Z-line and I-band.

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

10 0 nm (up to three regulatory units) into the I-band.

11 rational circular dichroism of the two amide I bands.

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

13 dapting the emission to cover only the amide I' band.

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

15 ity important for localizing mitochondria to I-bands.

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

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

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

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

20 seline correction and normalization to Amide-I band (~ 1650 cm(-1)).

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

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

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

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

25 ly, the ends of both proteins overlap at the I-band/A-band border, revealing a staggered organisation

26 the spectral range of the retinal and amide I bands across the time range from femtoseconds to secon

27 By contrast, due to a type-I band alignment and orthogonal orientation of the pai-s

28 t the MoSe(2)/WS(2) heterobilayer has a type I band alignment at large twist angles.

29 colocalization through the formation of type I band alignment at tensile-strained subregions.

30 Type-I band alignment ensures that the QDs are charge accepto

31 on between PbI(2) and these monolayers; type I band alignment in MoS(2) /PbI(2) stacks, where fast-tr

32 n the CsPbBr(3)/SLG/CsPbI(3), we find a type I band alignment that supports transfer of photogenerate

33 PbS domain was observed, pointing to a type-I band alignment, as confirmed by calculations.

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

35 us spatially modulated regions of local type I band alignment, hosting bright intralayer excitons, an

36 c state, these heterobilayers exhibit a type-I band alignment, resulting in the dominant intralayer e

37 y, seeking to implement lattice-matched type-I band alignment.

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

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

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

41 tructure modeling, we have assembled refined I-band and H-zone models with unparalleled scope and res

42 nown about the molecular organization of the I-band and H-zone.

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

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

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

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

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

48 teraction of actin and myosin in the A-band, I-band, and Z-disc and demonstrates that a-actinin cross

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

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

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

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

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

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

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

56 The collagen specific amide I band at 1665 cm(-1), has the higher sensitivity depend

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

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

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

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

61 Amide I band attenuated total reflection/Fourier transformed i

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

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

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

65 that 2D-IR spectroscopy of the protein amide I band can be performed in aqueous (H(2)O) rather than d

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

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

68 enhanced signal-to-noise ratio in the amide I band compared to the non-SAC results.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

83 ) is largely dictated by three key aspects: (i) band gap; (ii) absolute potentials of the conduction

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

85 ure shows interesting relationships to other I-band Ig domains.

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

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

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

89 r tensile strength and the presence of amide I bands in FTIR, indicating structural interactions.

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

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

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

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

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

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

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

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

98 While the amide I band is usually used to determine the secondary struct

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

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

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

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

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

104 lude that a titin-like dynamic spring in the I-band, made by an undamped elastic element in-series wi

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

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

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

108 he acquisition strategy to resolve the Amide I band needs to be identified.

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

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

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

112 cations in the secondary structure and amide I band of enzyme upon ligand binding.

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

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

115 , as manifested by the recovery of the amide-I band of monomeric Abeta, which is red-shifted by 26 cm

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

117 fted by 26 cm(-1) when compared to the amide-I band of the fibrillar form.

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

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

120 ardiac muscle and localize to the Z-disc and I band of the sarcomere.

121 In each case, spectral changes to the amide I band of the serum sample were observed, consistent wit

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

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

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

125 , extracted, and preprocessed, and the Amide I bands of the protein samples were compared and further

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

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

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

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

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

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

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

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

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

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

136 The I-band part of titin is elastic, and its constitutive im

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

168 the sarcomere by binding to titin N2A in the I-band region.

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

170 A common approach is band removal with conversion to another weight loss p

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

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

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

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

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

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

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

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

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

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

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

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

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

184 Its I-band segment, which includes the N2B element and the P

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

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

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

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

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

190 The stiffness and tunability of the I-band spring implicate titin as a force contributor tha

191 In this way, the I-band spring plays a fundamental role in preventing the

192 lament with the sarcomere end, working as an I-band spring that accounts for the rise of passive forc

193 C), we measure the undamped stiffness of an I-band spring that at SL > 2.7 um attains a maximum cons

194 ength 2.7-3.1 um, showing the ability of the I-band spring to adapt its length to the width of the I-

195 t fibres from frog skeletal muscle reveal an I-band spring with an undamped stiffness 100 times large

196 directed mutagenesis in titin that alter the I-band stiffness.

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

198 ring DCM-associated TTNtvs within A-band and I-band structural domains using induced pluripotent stem

199 activation at physiological SL, titin in the I-band switches from an SL-dependent extensible spring (

200 identified within the A-band and N-terminal I-band that closely correlated with regions of high perc

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

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

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

204 In this way, I-band titin efficiently transmits any load increase to

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

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

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

208 X-ray diffraction signals reveal that, with I-band titin ON, the periodic interactions of A-band tit

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

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

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

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

213 iminished sarcomere function greater than an I-band TTNtv in proportion to estimated DCM pathogenicit

214 of TTN truncation peptides using a proximal I-band TTNtv partially restored cardiac microtissue twit

215 peptides through introduction of a proximal I-band TTNtv, we studied genetic mechanisms in single ca

216 ain-binding domains are more pathogenic than I-band variants by incompletely understood mechanisms.

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

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

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

220 n, Sallimus bridges across the flight muscle I-band, whereas Projectin is located at the beginning of

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

222 hing more than 2 um to bridge the sarcomeric I-band, while Projectin covers almost the entire myosin

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

224 of H(2)O that overlap with the protein amide I band with analysis of peak patterns appearing in the o

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

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

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