High school agriculture / by D.D. Mayne and K.L. Hatch.

Hatch, Kirk Lester; Mayne, D. D.

doi:10.5962/bhl.title.31532

Cited by 5 publications

(8 citation statements)

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“…The AmI band frequency and intensity are sensitive to the dielectric constant and the hydrogen bonding of the amide carbonyl groups. [29][30][31][32][33][34][35] This makes the AmI band a spectral marker for examining the water exposure and hydrogen bonding of amide groups. 20,30 An environment with a large dielectric constant, such as water, increases the contribution of the amide dipolar resonance structure ( − O-C=NH + ) compared to that of the less-polar resonance structure (O=C-NH).…”

Section: Uvrr Methodsmentioning

confidence: 99%

“…This decreases the C=O bond force constant and the AmI frequency. 29,32 Also, stronger hydrogen bonding to the C=O bond decreases its bond force constant downshifting the AmI band frequency 29,30,34 .…”

Section: Uvrr Methodsmentioning

confidence: 99%

“…In general, the deep UVRR enhancement of the AmI band of primary and secondary amides decreases with an increasing dielectric constant and/or increased hydrogen bonding to the amide C=O group. 29,32 This occurs because resonance enhancement depends on the Frank-Condon overlap between the amide ground and resonant excited states. The resonance enhancement of the AmI vibration scales with the square of the displacement between the equilibrium C=O bond ground electronic state and the ππ*excited state along the AmI vibrational normal coordinate.…”

Section: Uvrr Methodsmentioning

confidence: 99%

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UV Resonance Raman Structural Characterization of an (In)soluble Polyglutamine Peptide

2019

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Fibrillization of polyglutamine (polyQ) tracts in proteins is implicated in at least 10 neurodegenerative diseases. This generates great interest in the structure and the aggregation mechanism(s) of polyQ peptides. The fibrillization of polyQ is thought to result from the peptide's insolubility in aqueous solutions; longer polyQ tracts show decreased aqueous solution solubility, which is thought to lead to faster fibrillization kinetics. However, few studies have characterized the structure(s) of polyQ peptides with low solubility. In the work here, we use UV resonance Raman spectroscopy to examine the secondary structures, backbone hydrogen bonding, and side chain hydrogen bonding for a variety of solution-state, solid, and fibril forms of D 2 Q 20 K 2 (Q20). Q20 is insoluble in water and has a β-strand-like conformation with extensive inter-and intrapeptide hydrogen bonding in both dry and aqueous environments. We find that Q20 has weaker backbone-backbone and backbone-side chain hydrogen bonding and is less ordered compared to that of polyQ fibrils. Interestingly, we find that the insoluble Q20 will form fibrils when incubated in water at room temperature for ~5 h. Also, Q20 can be prepared using a wellknown disaggregation procedure to produce a water-soluble PPII-like conformation with negligible inter-and intrapeptide hydrogen bonding and a resistance to aggregation.

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Section: Uvrr Methodsmentioning

confidence: 99%

Section: Uvrr Methodsmentioning

confidence: 99%

Section: Uvrr Methodsmentioning

confidence: 99%

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UV Resonance Raman Structural Characterization of an (In)soluble Polyglutamine Peptide

2019

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“…P0 chondrocytes were grown for 24 h and P1 chondrocytes were grown for 3 and 6 days, in the presence of 1% FBS supplemented or not with 100 ng/ml BMP-2 or 5 ng/ml TGF-L1. The cell cultures were then treated as previously described [33], followed by an incubation for 1 h with the 2B1 monoclonal antibody recognizing an epitope located in the triple helix of type II collagen [35], or with polyclonal rabbit antibodies raised against mouse type I collagen (Novotec ref. 20151) [36].…”

Section: Immuno£uorescencementioning

confidence: 99%

Alternative splicing of type II procollagen pre‐mRNA in chondrocytes is oppositely regulated by BMP‐2 and TGF‐β1

et al. 2003

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Type II collagen is the major protein of cartilage and is synthesized as a procollagen in two forms (IIA and IIB), generated by di¡erential splicing of the gene primary transcript. Previous studies have indicated that only type IIB is expressed in di¡erentiated chondrocytes. Here, we examined the e¡ects of bone morphogenetic protein (BMP)-2 and transforming growth factor (TGF)-L L1 on the expression of IIA and IIB forms expressed in de-di¡erentiated chondrocytes grown in monolayer. Our results demonstrate that BMP-2 favors expression of type IIB whereas TGF-L L1 potentiates expression of type IIA induced by subculture. These observations reveal the speci¢c capability of BMP-2 to reverse the de-di¡erentiation state of chondrocytes.

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“…In the present work, we functionalize graphene with a thin film of Pt-porphyrins. The first layer directly in contact with graphene can interact with graphene's delocalised sp 2 orbitals and is expected to form an ordered array [15]. Neutral Pt-porphyrins are non magnetic, but the ionized form carries a magnetic moment of one Bohr magneton [16].…”

Section: Introductionmentioning

confidence: 99%

Signature of gate-tunable magnetism in graphene grafted with Pt-porphyrins

Komatsu

Bertrand

et al. 2016

Phys. Rev. B

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Inducing magnetism in graphene holds great promises, such as controlling the exchange interaction with a gate electrode, and generating exotic magnetic phases. Coating graphene with magnetic molecules or atoms has so far mostly lead to decreased graphene mobility. In the present work, we show that Pt-porphyrin molecules adsorbed on graphene lead both to an enhanced mobility, and to gate-dependent magnetism. We report that porphyrins can act both as donor or acceptor molecules, depending on the initial doping of the graphene sheet. The porphyrins transfer charge and ionize around the charged impurities on graphene, and, consequently, the graphene doping is decreased and its mobility is enhanced.In addition, ionized porphyrin molecules carry a magnetic moment. Using the sensitivity of mesoscopic transport to magnetism, in particular the superconducting proximity effect and conductance fluctuations, we explore the magnetic order induced in graphene by the interacting magnetic moments of the ionized porphyrin molecules.Among the signatures of magnetism, we find two-terminal-magnetoresistance fluctuations with an odd component, a tell-tale sign of time reversal symmetry breaking at zero field, that does not exist in uncoated graphene samples. When graphene is connected to superconducting electrodes, the induced magnetism leads to a gate-voltage-dependent suppression of the supercurrent, modified magnetic interference patterns, and gate-voltage-dependent magnetic hysteresis. The magnetic signatures are greatest for long superconductor/graphene/superconductor junctions, and for samples with the highest initial doping, compatible with a greater number of ionized, and thus magnetic porphyrin molecules. Our findings suggest that long-range (of the order of the coherence length, or micrometers) magnetism is induced through graphene by the ionized porphyrins' magnetic moment. This magnetic interaction is controled by the density of carriers in graphene, a tunability that could be exploited in spintronic applications.

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High school agriculture / by D.D. Mayne and K.L. Hatch.

Cited by 5 publications

References 0 publications

UV Resonance Raman Structural Characterization of an (In)soluble Polyglutamine Peptide

UV Resonance Raman Structural Characterization of an (In)soluble Polyglutamine Peptide

Alternative splicing of type II procollagen pre‐mRNA in chondrocytes is oppositely regulated by BMP‐2 and TGF‐β1

Signature of gate-tunable magnetism in graphene grafted with Pt-porphyrins

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