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Recent Advance in Ionic‐Liquid‐Based Electrolytes for Rechargeable Metal‐Ion Batteries
From basic research to industry process, battery energy storage systems have played a great role in the informatization, mobility, and intellectualization of modern human society. Some potential systems such as Li, Na, K, Mg, Zn, and Al secondary batteries have attracted much attention to maintain social progress and sustainable development. As one of the components in batteries, electrolytes play an important role in the upgrade and breakthrough of battery technology. Since room‐temperature ionic liquids (ILs) feature high conductivity, nonflammability, nonvolatility, high thermal stability, and wide electrochemical window, they have been widely applied in various battery systems and show great potential in improving battery stability, kinetics performance, energy density, service life, and safety. Thus, it is a right time to summarize these progresses. In this review, the composition and classification of various ILs and their recent applications as electrolytes in diverse metal‐ion batteries (Li, Na, K, Mg, Zn, Al) are outlined to enhance the battery performances. This manuscript reviews the classification of ionic liquids, and their potential application as electrolytes in metal‐ion batteries (Li, Na, K, Mg, Zn, Al). Their merits of nonflammable property, thermal stability, and high safety suggest that they could be a promising solution to realize high safety and high energy density for next generational battery systems.
Journal Article
The handbook of lithium-ion battery pack design : chemistry, components, types and terminology
'The Handbook of Lithium-Ion Battery Pack Design' offers to the reader a clear and concise explanation of how Li-ion batteries are designed from the perspective of a manager, sales person, product manager or entry level engineer who is not already an expert in Li-ion battery design. It will offer a layman's explanation of the history of vehicle electrification, what the various terminology means, and how to do some simple calculations that can be used in determining basic battery sizing, capacity, voltage and energy. By the end of this book the reader has a solid understanding of all of the terminology around Li-ion batteries and is able to do some simple battery calculations.
Book
Structural basis for Na+ transport mechanism by a light-driven Na+ pump
Krokinobacter eikastus
rhodopsin 2 (KR2) is the first light-driven Na
+
pump discovered, and is viewed as a potential next-generation optogenetics tool. Since the positively charged Schiff base proton, located within the ion-conducting pathway of all light-driven ion pumps, was thought to prohibit the transport of a non-proton cation, the discovery of KR2 raised the question of how it achieves Na
+
transport. Here we present crystal structures of KR2 under neutral and acidic conditions, which represent the resting and M-like intermediate states, respectively. Structural and spectroscopic analyses revealed the gating mechanism, whereby the flipping of Asp116 sequesters the Schiff base proton from the conducting pathway to facilitate Na
+
transport. Together with the structure-based engineering of the first light-driven K
+
pumps, electrophysiological assays in mammalian neurons and behavioural assays in a nematode, our studies reveal the molecular basis for light-driven non-proton cation pumps and thus provide a framework that may advance the development of next-generation optogenetics.
KR2 light-driven Na
+
pump structure
Known microbial rhodopsins were classified into two groups, either outward proton pumps or inward chloride pumps, until the recent discovery of a light-driven Na
+
-pumping rhodopsin from the marine bacterium
Krokinobacter eikastus
. This novel protein, termed KR2, is attracting attention as a potential tool for use in optogenetics: its activation would change the sodium concentration of a targeted cell, not just the pH or chloride concentration. Now Osamu Nureki and colleagues have solved two X-ray crystal structures of KR2 and they use them to propose a working model for Na
+
transport. Based on these structures the authors have designed several mutants of KR2 and successfully engineered a K
+
-transporting pump.
Journal Article
Structure of the mechanically activated ion channel Piezo1
Piezo1 and Piezo2 are mechanically activated ion channels that mediate touch perception, proprioception and vascular development. Piezo proteins are distinct from other ion channels and their structure remains poorly defined, which impedes detailed study of their gating and ion permeation properties. Here we report a high-resolution cryo-electron microscopy structure of the mouse Piezo1 trimer. The detergent-solubilized complex adopts a three-bladed propeller shape with a curved transmembrane region containing at least 26 transmembrane helices per protomer. The flexible propeller blades can adopt distinct conformations, and consist of a series of four-transmembrane helical bundles that we term Piezo repeats. Carboxy-terminal domains line the central ion pore, and the channel is closed by constrictions in the cytosol. A kinked helical beam and anchor domain link the Piezo repeats to the pore, and are poised to control gating allosterically. The structure provides a foundation to dissect further how Piezo channels are regulated by mechanical force.
The cryo-electron microscopy structure of full-length mouse Piezo1 reveals six Piezo repeats, and 26 transmembrane helices per protomer, and shows that a kinked helical beam and anchor domain link the Piezo repeats to the pore and control gating allosterically.
Structure and mechanism of ion channel Piezo1
Mechanosensitive cation channels convert external mechanical stimuli into various biological actions, including touch, hearing, balance and cardiovascular regulation. The eukaryotic Piezo proteins are mechanotransduction channels, although their structure and gating mechanisms are not well elucidated. In related papers in this issue of
Nature
, two groups report cryo-electron microscopy structures of the full-length mouse Piezo1 and reveal three flexible propeller blades. Each blade is made up of at least 26 helices, forming a series of helical bundles, which adopt a curved transmembrane region. A kinked beam and anchor domain link these Piezo repeats to the pore, giving clues as to how the channel responds to membrane tension and mechanical force.
Journal Article
The pH scale
\"The pH scale measures how acidic or basic a substance is, ranging from 0 to 14. Readers will learn how certain substances rank on the pH scale, what happens when acids and bases are mixed, and how water can make a substance either acidic or basic. These significant science concepts are discussed in clear and approachable text and supported by motivating fact boxes, charts, and images and photographs.\"-- Provided by publisher.
Book
The His-Gly motif of acid-sensing ion channels resides in a reentrant ‘loop’ implicated in gating and ion selectivity
Acid-sensing ion channels (ASICs) are proton-gated members of the epithelial sodium channel/degenerin (ENaC/DEG) superfamily of ion channels and are expressed throughout the central and peripheral nervous systems. The homotrimeric splice variant ASIC1a has been implicated in nociception, fear memory, mood disorders and ischemia. Here, we extract full-length chicken ASIC1 (cASIC1) from cell membranes using styrene maleic acid (SMA) copolymer, elucidating structures of ASIC1 channels in both high pH resting and low pH desensitized conformations by single-particle cryo-electron microscopy (cryo-EM). The structures of resting and desensitized channels reveal a reentrant loop at the amino terminus of ASIC1 that includes the highly conserved ‘His-Gly’ (HG) motif. The reentrant loop lines the lower ion permeation pathway and buttresses the ‘Gly-Ala-Ser’ (GAS) constriction, thus providing a structural explanation for the role of the His-Gly dipeptide in the structure and function of ASICs.
Journal Article
diaPASEF: parallel accumulation–serial fragmentation combined with data-independent acquisition
Data-independent acquisition modes isolate and concurrently fragment populations of different precursors by cycling through segments of a predefined precursor
m/z
range. Although these selection windows collectively cover the entire
m/z
range, overall, only a few per cent of all incoming ions are isolated for mass analysis. Here, we make use of the correlation of molecular weight and ion mobility in a trapped ion mobility device (timsTOF Pro) to devise a scan mode that samples up to 100% of the peptide precursor ion current in
m/z
and mobility windows. We extend an established targeted data extraction workflow by inclusion of the ion mobility dimension for both signal extraction and scoring and thereby increase the specificity for precursor identification. Data acquired from whole proteome digests and mixed organism samples demonstrate deep proteome coverage and a high degree of reproducibility as well as quantitative accuracy, even from 10 ng sample amounts.
diaPASEF makes use of the correlation between the ion mobility and the
m
/
z
of peptides to trap and release precursor ions in a TIMS-TOF mass spectrometer for an almost complete sampling of the precursor ion beam with data-independent acquisition.
Journal Article