RESUMO
Despite its disordered liquid-like structure, glass exhibits solid-like mechanical properties1. The formation of glassy material occurs by vitrification, preventing crystallization and promoting an amorphous structure2. Glass is fundamental in diverse fields of materials science, owing to its unique optical, chemical and mechanical properties as well as durability, versatility and environmental sustainability3. However, engineering a glassy material without compromising its properties is challenging4-6. Here we report the discovery of a supramolecular amorphous glass formed by the spontaneous self-organization of the short aromatic tripeptide YYY initiated by non-covalent cross-linking with structural water7,8. This system uniquely combines often contradictory sets of properties; it is highly rigid yet can undergo complete self-healing at room temperature. Moreover, the supramolecular glass is an extremely strong adhesive yet it is transparent in a wide spectral range from visible to mid-infrared. This exceptional set of characteristics is observed in a simple bioorganic peptide glass composed of natural amino acids, presenting a multi-functional material that could be highly advantageous for various applications in science and engineering.
Assuntos
Adesivos , Vidro , Oligopeptídeos , Adesivos/química , Vidro/química , Temperatura , Vitrificação , Água/química , Oligopeptídeos/química , Tirosina/química , Luz , Raios InfravermelhosRESUMO
Rotor-synchronous π pulses applied to protons (S) enhance homonuclear polarisation transfer between two spins (I) such as 13C or 15N as long as at least a single I-S heteronuclear dipolar-coupling interaction exists. The enhancement is maximum when the chemical-shift difference Δν between two spins equals an integer multiple, n, of the pulse-modulation frequency, which is half the rotor frequency νr. This condition, applied in the Pulse Induced Resonance with Angular dependent Total Enhancement (PIRATE) experiment, can be generalised for any spacing of the pulses k/νr such that Δν=nνr2k . We show, using average Hamiltonian theory (AHT) and Floquet theory, that the resonance conditions promote a second-order recoupling consisting of a cross-term between the homonuclear and heteronuclear dipolar interactions in a three-spin system. The minimum requirement is a coupling between the two I spins and a coupling of one of the I spins to the S spin. The effective Hamiltonian at the resonance conditions contains three-spin operators of the form 2I1±I2∓Sz with a non-zero effective dipolar coupling. Theoretical analysis shows that the effective strength of the resonance conditions decreases with increasing values of k and n. The theory is backed by numerical simulations, and experimental results on fully labelled 13C-glycine demonstrating the efficiency of the different resonance condition for k=1,2 at various spinning frequencies.
RESUMO
An important step in the process of protein research by NMR is the assignment of chemical shifts. In the coat protein of IKe bacteriophage, there are 53 residues making up a long helix resulting in relatively high spectral ambiguity. Assignment thus requires the collection of a set of three-dimensional (3D) experiments and the preparation of sparsely labeled samples. Increasing the dimensionality can facilitate fast and reliable assignment of IKe and of larger proteins. Recent progress in nonuniform sampling techniques made the application of multidimensional NMR solid-state experiments beyond 3D more practical. 4D 1 H-detected experiments have been demonstrated in high-fields and at spinning speeds of 60 kHz and higher but are not practical at spinning speeds of 10-20 kHz for fully protonated proteins. Here, we demonstrate the applicability of a nonuniformly sampled 4D 13 C/15 N-only correlation experiment performed at a moderate field of 14.1 T, which can incorporate sufficiently long acquisition periods in all dimensions. We show how a single CANCOCX experiment, supported by several 2D carbon-based correlation experiments, is utilized for the assignment of heteronuclei in the coat protein of the IKe bacteriophage. One sparsely labeled sample was used to validate sidechain assignment of several hydrophobic-residue sidechains. A comparison to solution NMR studies of isolated IKe coat proteins embedded in micelles points to key residues involved in structural rearrangement of the capsid upon assembly of the virus. The benefits of 4D to a quicker assignment are discussed, and the method may prove useful for studying proteins at relatively low fields.
Assuntos
Bacteriófago IKe/química , Proteínas do Capsídeo/análise , Capsídeo/química , Proteínas do Capsídeo/química , Espectroscopia de Ressonância Magnética Nuclear de Carbono-13 , Micelas , Isótopos de Nitrogênio/química , Ressonância Magnética Nuclear Biomolecular , Conformação Proteica em alfa-HéliceRESUMO
Polycrystalline bis(dialkyldithiophosphato)Pt(II) complexes of the form [Pt{S2P(OR)2}2] (R = ethyl, iso-propyl, iso-butyl, sec-butyl or cyclo-hexyl group) were studied using solid-state 31P and 195Pt NMR spectroscopy, to determine the influence of R to the structure of the central chromophore. The measured anisotropic chemical shift (CS) parameters for 31P and 195Pt afford more detailed chemical and structural information, as compared to isotropic CS and J couplings alone. Advanced theoretical modeling at the hybrid DFT level, including both crystal lattice and the important relativistic spin-orbit effects qualitatively reproduced the measured CS tensors, supported the experimental analysis, and provided extensive orientational information. A particular correction model for the non-negligible lattice effects was adopted, allowing one to avoid a severe deterioration of the 195Pt anisotropic parameters due to the high requirements posed on the pseudopotential quality in such calculations. Though negligible differences were found between the 195Pt CS tensors with different substituents R, the 31P CS parameters differed significantly between the complexes, implying the potential to distinguish between them. The presented approach enables good resolution and a detailed analysis of heavy-element compounds by solid-state NMR, thus widening the understanding of such systems.
RESUMO
This study demonstrates the utility of the novel Field Sweep Fourier Transform (FSFT) method for acquiring wideline (195)Pt NMR data from various sized Pt nanoparticles, Pt-Sn intermetallics/bimetallics used to catalyse oxidative processes in fuel cell applications, and various other related Pt3X alloys (X = Al, Sc, Nb, Ti, Hf and Zr) which can facilitate oxygen reduction catalysis. The (195)Pt and (119)Sn NMR lineshapes measured from the PtSn intermetallic and Pt3Sn bimetallic systems suggest that these are more ordered than other closely related bimetallic alloys; this observation is supported by other characterisation techniques such as XRD. From these reconstructed spectra the mean number of atoms in a Pt nanoparticle can be accurately determined, along with detailed information regarding the number of atoms present effectively in each layer from the surface. This can be compared with theoretical predictions of the number of Pt atoms in these various layers for cubo-octahedral nanoparticles, thereby providing an estimate of the particle size. A comparison of the common NMR techniques used to acquire wideline data from the I = 1/2 (195)Pt nucleus illustrates the advantages of the automated FSFT technique over the Spin Echo Height Spectroscopy (SEHS) (or Spin Echo Integration Spectroscopy (SEIS)) approach that dominates the literature in this area of study. This work also presents the first (195)Pt NMR characterisation of novel small Pt13 nanoclusters which are diamagnetic and thus devoid of metallic character. This unique system provides a direct measure of an isotropic chemical shift for these Pt nanoparticles and affords a better basis for determining the actual Knight shift when compared to referencing against the primary IUPAC shift standard (1.2 M Na2PtCl6(aq)) which has a very different local chemical environment.
RESUMO
A pioneer of veterinary radiology, she was a born teacher and a role model.
RESUMO
We demonstrate a new resonance condition that obeys the relation Δδ=nνR/2, where Δδ is the chemical shift difference between two homonuclear-coupled spins, νR is the magic-angle spinning speed and n is an integer. This modulation on the rotational resonance recoupling condition is obtained by the application of rotor-synchronous 1H pulses when at least one proton is dipolar-coupled to one of the homonuclear spins. We suggest a new experimental scheme entitled 'pulse induced resonance with angular dependent total enhancement' (PIRATE) that can enhance proton-driven spin diffusion by the application of a single 1H pulse every rotor period. Experimental evidence is demonstrated on the two carbon spins of glycine and on the Y21M mutant of fd bacteriophage virus. Numerical simulations reveal the existence of the resonances and report on the important interactions governing these phenomena.
Assuntos
Imageamento por Ressonância Magnética , Prótons , Glicina/química , Frequência Cardíaca , Espectroscopia de Ressonância Magnética/métodosRESUMO
RNA is a polymer with pivotal functions in many biological processes. RNA structure determination is thus a vital step toward understanding its function. The secondary structure of RNA is stabilized by hydrogen bonds formed between nucleotide basepairs, and it defines the positions and shapes of functional stem-loops, internal loops, bulges, and other functional and structural elements. In this work, we present a methodology for studying large intact RNA biomolecules using homonuclear 15N solid-state NMR spectroscopy. We show that proton-driven spin-diffusion experiments with long mixing times, up to 16 s, improved by the incorporation of multiple rotor-synchronous 1H inversion pulses (termed radio-frequency dipolar recoupling pulses), reveal key hydrogen-bond contacts. In the full-length RNA isolated from MS2 phage, we observed strong and dominant contributions of guanine-cytosine Watson-Crick basepairs, and beyond these common interactions, we observe a significant contribution of the guanine-uracil wobble basepairs. Moreover, we can differentiate basepaired and non-basepaired nitrogen atoms. Using the improved technique facilitates characterization of hydrogen-bond types in intact large-scale RNA using solid-state NMR. It can be highly useful to guide secondary structure prediction techniques and possibly structure determination methods.