Relevant bibliographies by topics / Helix 38

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  3. Conference papers

Academic literature on the topic 'Helix 38'

Author: Grafiati
Published: 4 June 2021
Last updated: 1 February 2022

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Journal articles on the topic "Helix 38"

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Moroz, P. E. "Novel stellarator configuration with double helix centre post." Nuclear Fusion 38, no. 6 (June 1998): 795–806. http://dx.doi.org/10.1088/0029-5515/38/6/302.

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Sonief, Achmad As'ad, Arda Nur Fauzan, Fachry Azlan, and Muhammad Aziz Bashori. "Chatter Vibration Comparison Between Normal Helix Angle and Variable Helix Angle in End Milling Process Based on Spectrum Analysis." Jurnal Rekayasa Mesin 11, no. 3 (December 15, 2020): 531–36. http://dx.doi.org/10.21776/ub.jrm.2020.011.03.25.

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Chatter vibration in machining processes is often found in cutting processes which will decrease the machining efficiency and the surface quality of the products. Chatter is a relative vibration of the cutting tool and workpiece caused by the fluctuation of cutting force that is concerned to be a self-excited vibration. The variable Helix Angle Cutting tool which has pitch angle variation will also inflict different tooth passing frequencies on the flute that stand contiguous and trim the resonance frequency. This research aims to compare chatter vibrations that occurred between Normal Helix Angle and Variable Helix Angle cutting tool based on spectrum analysis on cutting parameter variety (depth of cut; rotation speed; feed rate milling). The outcome is spectrum analysis can detect the chatter phenomenon, measure the natural frequency (38-42 Hz), and also compare chatter vibrations between two tools appropriately.
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Rastelli, E., S. Sedazzari, and A. Tassi. "The helix-fan transition in the square planar model." Journal of Physics: Condensed Matter 5, no. 38 (September 20, 1993): 7121–30. http://dx.doi.org/10.1088/0953-8984/5/38/008.

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Rakauskaite, Rasa, and Jonathan D. Dinman. "An Arc of Unpaired “Hinge Bases” Facilitates Information Exchange among Functional Centers of the Ribosome." Molecular and Cellular Biology 26, no. 23 (September 25, 2006): 8992–9002. http://dx.doi.org/10.1128/mcb.01311-06.

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ABSTRACT Information must be shared and functions coordinated among the spatially distinct functional centers of the ribosome. To address these issues, a yeast-based genetic system enabling generation of stable strains expressing only mutant forms of rRNA was devised. The B1a bridge (helix 38) has been implicated in the subtle modulation of numerous ribosomal functions. Base-specific mutations were introduced into helix 38 at sites affecting the B1a bridge and where it contacts the aminoacyl-tRNA (aa-tRNA) D-loop. Both sets of mutants promoted increased affinities for aa-tRNA but had different effects in their responses to two A-site-specific drugs and on suppression nonsense codons. Structural analyses revealed an arc of nucleotides in 25S rRNA that link the B1a bridge, the peptidyltransferase center, the GTPase-associated center, and the sarcin/ricin loop. We propose that a series of regularly spaced “hinge bases” provide fulcrums around which rigid helices can reorient themselves depending on the occupancy status of the A-site.
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Maeda, Yasushi, Takuya Matsumoto, Hiroyuki Tanaka, and Tomoji Kawai. "Imaging of the DNA (deoxyribonucleic acid) Double Helix Structure by Noncontact Atomic Force Microscopy." Japanese Journal of Applied Physics 38, Part 2, No. 11A (November 1, 1999): L1211—L1212. http://dx.doi.org/10.1143/jjap.38.l1211.

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Perera, Rushika, Chanakha Navaratnarajah, and Richard J. Kuhn. "A Heterologous Coiled Coil Can Substitute for Helix I of the Sindbis Virus Capsid Protein." Journal of Virology 77, no. 15 (August 1, 2003): 8345–53. http://dx.doi.org/10.1128/jvi.77.15.8345-8353.2003.

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ABSTRACT Alphavirus core assembly proceeds along an assembly pathway involving a dimeric assembly intermediate. Several regions of the alphavirus capsid protein have been implicated in promoting and stabilizing this dimerization, including a putative heptad repeat sequence named helix I. This sequence, which spans residues 38 to 55 of the Sindbis virus capsid protein, was implicated in stabilizing dimeric contacts initiated through the C-terminal two-thirds of the capsid protein and nucleic acid. The studies presented here demonstrate that helix I can be functionally replaced by the corresponding sequence of a related alphavirus, western equine encephalitis virus, and also by an unrelated sequence from the yeast transcription activator, GCN4, that was previously shown to form a dimeric coiled coil. Replacing helix I with the entire leucine zipper domain of GCN4 (residues 250 to 281) produced a virus with the wild-type phenotype as determined by plaque assay and one-step growth analysis. However, replacement of helix I with a GCN4 sequence that favored trimer formation produced a virus that exhibited ∼40-fold reduction in virus replication compared to the wild-type Sindbis virus. Changing residues within the Sindbis virus helix I sequence to favor trimer formation also produced a virus with reduced replication. Peptides corresponding to helix I inhibited core-like particle assembly in vitro. On the basis of these studies, it is proposed that helix I favors capsid protein-capsid protein interactions through the formation of dimeric coiled-coil interactions and may stabilize assembly intermediates in the alphavirus nucleocapsid core assembly pathway.
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Kanno, Takashi, Hiroyuki Tanaka, Tomohiko Nakamura, Hitoshi Tabata, and Tomoji Kawai. "Real Space Observation of Double-Helix DNA Structure Using a Low Temperature Scanning Tunneling Microscopy." Japanese Journal of Applied Physics 38, Part 2, No. 6A/B (June 15, 1999): L606—L607. http://dx.doi.org/10.1143/jjap.38.l606.

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8

Andre Hardinsi, Festo, Oyong Novareza, and Achmad As'ad Sonief. "OPTIMIZATION OF VARIABEL HELIX ANGLE PARAMETERS IN CNC MILLING OF CHATTER AND SURFACE ROUGHNES USING TAGUCHI METHOD." Journal of Engineering and Management in Industrial System 9, no. 1 (May 30, 2021): 35–44. http://dx.doi.org/10.21776/ub.jemis.2021.009.01.4.

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In the manufacturing industries, the main problem in process of operating CNC milling machine was chatter effect (self-excited vibration) which increases the quality of the surface roughness. In this study is to determine optimal value of parameters for chatter and surface roughness. The chatter measured using accelerometer MPU-6050 with Arduino by software LabVIEW-2019 based on peaks-FFT value and the surface roughness measured by SJ-301 tester. The research parameters like variable helix angle, spindle speed, feed rate, and depth of cut using stainless steel 304 by Taguchi method. The optimum parameters value obtained are variable helix 35/38 degrees, spindle speed 3000 RPM, feed rate 150 mm/min and depth of cut 0.4 mm. Based on ANOVA value, the variable helix angle and depth of cut are found to be significant for chatter and surface roughness. The depth of cut was high contribution by ANOVA chatter by 93.84% and surface roughness by 91.93%.
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Perera, Rushika, Katherine E. Owen, Timothy L. Tellinghuisen, Alexander E. Gorbalenya, and Richard J. Kuhn. "Alphavirus Nucleocapsid Protein Contains a Putative Coiled Coil α-Helix Important for Core Assembly." Journal of Virology 75, no. 1 (January 1, 2001): 1–10. http://dx.doi.org/10.1128/jvi.75.1.1-10.2001.

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ABSTRACT The alphavirus nucleocapsid core is formed through the energetic contributions of multiple noncovalent interactions mediated by the capsid protein. This protein consists of a poorly conserved N-terminal region of unknown function and a C-terminal conserved autoprotease domain with a major role in virion formation. In this study, an 18-amino-acid conserved region, predicted to fold into an α-helix (helix I) and embedded in a low-complexity sequence enriched with basic and Pro residues, has been identified in the N-terminal region of the alphavirus capsid proteins. In Sindbis virus, helix I spans residues 38 to 55 and contains three conserved leucine residues, L38, L45, and L52, conforming to the heptad amino acid organization evident in leucine zipper proteins. Helix I consists of an N-terminally truncated heptad and two complete heptad repeats with β-branched residues and conserved leucine residues occupying the a andd positions of the helix, respectively. Complete or partial deletion of helix I, or single-site substitutions at the conserved leucine residues (L45 and L52), caused a significant decrease in virus replication. The mutant viruses were more sensitive to elevated temperature than wild-type virus. These mutant viruses also failed to accumulate cores in the cytoplasm of infected cells, although they did not have defects in protein translation or processing. Analysis of these mutants using an in vitro assembly system indicated that the majority were defective in core particle assembly. Furthermore, mutant proteins showed a trans-dominant negative phenotype in in vitro assembly reactions involving mutant and wild-type proteins. We propose that helix I plays a central role in the assembly of nucleocapsid cores through coiled coil interactions. These interactions may stabilize subviral intermediates formed through the interactions of the C-terminal domain of the capsid protein and the genomic RNA and contribute to the stability of the virion.
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Tsueshita, Takaya, Salil Gandhi, Hayat Önyüksel, and Israel Rubinstein. "Phospholipids modulate the biophysical properties and vasoactivity of PACAP-(1—38)." Journal of Applied Physiology 93, no. 4 (October 1, 2002): 1377–83. http://dx.doi.org/10.1152/japplphysiol.00277.2002.

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The purpose of this study was to elucidate the interactions between pituitary adenylate cyclase-activating peptide (PACAP)-(1—38) and phospholipids in vitro and to determine whether these phenomena modulate, in part, the vasorelaxant effects of the peptide in the intact peripheral microcirculation. We found that the critical micellar concentration of PACAP-(1—38) was 0.4–0.9 μM. PACAP-(1—38) significantly increased the surface tension of a dipalmitoylphosphatidylcholine monolayer and underwent conformational transition from predominantly random coil in saline to α-helix in the presence of distearoyl-phosphatidylethanolamine-polyethylene glycol (molecular mass of 2,000 Da) sterically stabilized phospholipid micelles (SSM) ( P < 0.05). Using intravital microscopy, we found that aqueous PACAP-(1—38) evoked significant concentration-dependent vasodilation in the intact hamster cheek pouch that was significantly potentiated when PACAP-(1—38) was associated with SSM ( P < 0.05). The vasorelaxant effects of aqueous PACAP-(1—38) were mediated predominantly by PACAP type 1 (PAC1) receptors, whereas those of PACAP-(1—38) in SSM predominantly by PACAP/vasoactive intestinal peptide type 1 and 2 (VPAC1/VPAC2) receptors. Collectively, these data indicate that PACAP-(1—38) self-associates and interacts avidly with phospholipids in vitro and that these phenomena amplify peptide vasoactivity in the intact peripheral microcirculation.
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Dissertations / Theses on the topic "Helix 38"

1

Crandall, Jacob N. "Ribosomal RNA Mutations that Inhibit the Activity of Transfer-Messenger RNA of Stalled Ribosomes." Diss., CLICK HERE for online access, 2010. http://contentdm.lib.byu.edu/ETD/image/etd3535.pdf.

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Conference papers on the topic "Helix 38"

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Batista, Michael, Hadi T. Nia, Karen Cox, Christine Ortiz, Alan J. Grodzinsky, Dick Heinegård, and Lin Han. "Effects of Chondroadherin on Cartilage Nanostructure and Biomechanics via Murine Model." In ASME 2013 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2013. http://dx.doi.org/10.1115/sbc2013-14516.

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While small leucine rich proteins/proteoglycans (SLRPs) are present in very low concentrations in the extracellular matrix (ECM), they have been shown to be critical determinants of the proper ECM assembly and function in connective tissues [1] including bone [2], cornea [3], and cartilage [4]. However, their direct and indirect roles in matrix biomechanics and the potential for osteoarthritis-related dysfunction of cartilage remain unclear. With the advent of new high resolution nanotechnological tools, the direct quantification of cartilage biomechanical properties using murine models can provide important insights into how secondary ECM molecules, such as SLRPs, affect the function and pathology of cartilage [5]. Previous nanoindentation studies of murine cartilage have assessed the effects of maturation and osteoarthritis-like degradation of cartilage on its biomechanical properties [6, 7]. Recently, murine models have received increased attention because of the availability of specific gene-knockout and gene alteration technologies [8]. For example, chondroadherin (CHAD) is a non-collagenous small leucine-rich proteoglycan (SLRP) with α-helix and β-sheet secondary structure, spatially localized in the territorial matrix (MW = 38 kDa) [9]. In articular cartilage, CHAD is distributed non-uniformly with depth [10], and binds to type II collagen and the α2β1 integrin and is hypothesized to function in the communication between chondrocytes and their surrounding matrix, as well as in the regulation of collagen fibril assembly [11, 12] (Fig. 1). The objective of the present study is to explore the role of CHAD and its depletion on the structure and nanomechanical properties of both superficial and middle/deep zone cartilage. The current methods thereby enabled depth-dependent analysis of cartilage nanostructure and dynamic energy-dissipative mechanisms.
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