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A 2,4-Diazadiboretidine contains an alternating four-membered B–N–B–N ring. nitrogen lone pairs provide sigma-donor sites, while the ring can bind an electron-rich metal through a pi interaction involving both B and N.

2-Picolylamine is pyridin-2-ylmethanamine, with a pyridine nitrogen and an aminomethyl nitrogen adjacent on the ring. It binds as an unsymmetrical neutral bidentate ligand, forming a five-membered chelate ring.

Acetonitrile, $\mathrm{C}{\mathrm{H}}_3\mathrm{CN}$, can coordinate through nitrogen as a neutral two-electron donor. Bound acetonitrile can be displaced by a stronger donor or an intramolecular chelating group.

ARKIVOC 2008(v), 136–152. nitrogen-bound adducts, unequal ring bonds and variable-temperature NMR in related borazines. The trialkylborazine measurements are analogues, not measurements of the hexamethyl compound.

Here an amide means a carbonyl group whose carbon is bonded directly to nitrogen; each of $R$, $R^{\prime }$ and $R^{\prime \prime }$ may be hydrogen or a group attached through carbon. A peptide bond contains this linkage. Chemical resonance distinguishes its nitrogen from that of an amine. ^[ref] and ^[ref]

An amido ligand contains an anionic nitrogen donor, such as $\mathrm{N}{\mathrm{R}}_2^{-}$. A neutral secondary amine retaining its N–H bond is a different donor type; confusing them changes formal metal oxidation state.

A simple neutral amine has nitrogen bonded to one, two, or three groups attached through carbon, with hydrogen filling the remaining positions in the neutral three-bond form. These are the primary, secondary, and tertiary forms respectively. An amide has different connectivity to a carbonyl group. ^[ref]

An amino acid combines carboxylic acid and amine functionality in the same molecule; the name alone does not specify their separation. An alpha-amino acid has its amino nitrogen attached to the carbon immediately adjacent to the carboxyl carbon, the amino acid alpha carbon. For example, ${\mathrm{H}}_2\mathrm{N}-\mathrm{C}{\mathrm{H}}_2-\mathrm{COOH}$ is glycine, whereas ${\mathrm{H}}_2\mathrm{N}-\mathrm{C}{\mathrm{H}}_2-\mathrm{C}{\mathrm{H}}_2-\mathrm{COOH}$ has an extra intervening carbon and is not an alpha-amino acid. These chemical formulas describe connectivity, not the predominant protonation state in water.

Most common proteinogenic amino acids share the skeleton ${\mathrm{H}}_2\mathrm{N}-\mathrm{CH}(R)-\mathrm{COOH}$, with $R$ the amino acid side chain. In glycine, $R$ is hydrogen; in alanine, $R=\mathrm{C}{\mathrm{H}}_3$. Proline is a useful exception to the displayed primary-amine skeleton: its amino nitrogen is part of a ring and has a second carbon substituent. The shared backbone permits assembly into polypeptides, while different amino acid side chains give the resulting proteins diverse chemistry. ^[ref]

In a chemical solution, protonation changes the electric charges without changing this backbone. Free glycine near neutral pH is predominantly ${\mathrm{H}}_3{\mathrm{N}}^{+}-\mathrm{C}{\mathrm{H}}_2-\mathrm{CO}{\mathrm{O}}^{-}$, a zwitterion. Its positive and negative groups are joined within one molecule; zero net electric charge does not mean absence of local electric charges, nor does it mean the uncharged drawing ${\mathrm{H}}_2\mathrm{N}-\mathrm{C}{\mathrm{H}}_2-\mathrm{COOH}$ predominates. Glycine protonation explains how lowering or raising pH changes the balance. ^[ref]

Building a protein joins the carboxyl carbon of one amino acid to the amino nitrogen of another through a peptide bond, an amide linkage. The formal net condensation loses the elements of water; cellular translation uses activated substrates at a ribosome, rather than simply mixing free amino acids in water. Incorporated units are amino acid residues. The interior amide groups no longer have the same acid/base behavior as the two free terminal groups of glycine, so its free-molecule glycine titration cannot be copied independently at every chain position. ^[ref]

Chirality distinguishes most common proteinogenic amino acids from glycine. The other nineteen members of the conventional twenty have a stereocenter at their amino acid alpha carbon; ordinary translation incorporates their L forms. Glycine's two identical hydrogen substituents make it achiral. Thus being an amino acid, or even an alpha-amino acid, does not by itself imply chirality. ^[ref]

In ammonia, the nitrogen chemical atom can lie on either side of the plane of the three hydrogen chemical atoms. Quantum tunnelling couples these configurations; the resulting pair of energy levels permits an electric dipole transition. This geometrical inversion is distinct from population inversion, which concerns how many molecules occupy each level.^[ref]

For an idealized pair of energy levels with equal quantum degeneracy, the Boltzmann distribution gives $N_u/N_l=\exp [-h{\nu }_0/(k_{\mathrm{B}}T)]<1$ at positive temperature $T$. A warm source therefore supplies upper-state molecules together with an unwanted lower-state population. Selecting the former can produce population inversion in the transmitted beam without exciting each transmitted molecule during selection. The energy per net downward transition isHere $h$ is the Planck constant. Taking the reported ${\nu }_0=23.87\mathrm{GHz}$ as a rounded input gives $ϵ\approx 1.582\times 10^{-23}\mathrm{J}$. This calculation is a conversion of the reported frequency, not a new measurement of the ammonia inversion transition.

An anilinium ion is an aniline protonated at nitrogen. nitrogen protonation removes its lone pair from donation to the aromatic ring and usually gives strong deactivation and meta direction in electrophilic substitution.

A carbon substituent opposite the activated N–O leaving group migrates onto nitrogen as the N–O bond cleaves. The oxime geometry therefore determines which bond is replaced by a carbon–nitrogen bond.

Consider an original simplified model containing only nitrogen and argon, with argon mole fraction $x$. Let their molar masses be $M_N$ and $M_A$. Adding the component masses gives the mixture's mean molar massFor an ideal gas mixture at the same pressure and temperature as a pure-nitrogen reference, the gas density ratio isThe inversion requires known identities, the binary-mixture assumption and $M_A\ne M_N$. A density ratio cannot uniquely recover an arbitrary multicomponent mixture. Nor should $x$ be interpreted as the argon fraction of untreated air: the model sample has only the two specified components.

Choose round model values $M_N=28\mathrm{g}\mathrm{mo}{\mathrm{l}}^{-1}$ and $M_A=40\mathrm{g}\mathrm{mo}{\mathrm{l}}^{-1}$. For $x=0.010$, the calculated relative density excess isThus a one-percent mole fraction does not mean a one-percent gas density change. In a chosen $2.00\mathrm{L}$ globe at $100\mathrm{kPa}$ and $300\mathrm{K}$, the ideal gas law gives approximately $2.24508\mathrm{g}$ for pure nitrogen and $2.25471\mathrm{g}$ for this mixture: only $9.62\mathrm{mg}$ separates the weighings. These are model calculations with rounded molar masses, not historical measurements.

A direct control calculation explains why the filling conditions matter. At fixed pressure, pure nitrogen athas the same gas density as that mixture at $300\mathrm{K}$. A roughly $1.28\mathrm{K}$ mismatch can therefore imitate the entire stipulated composition signal. For small changes, the ideal gas law givesAn independently measured pressure and temperature, matched weighing procedure, and checks for residual vapour distinguish composition from these alternative causes. The model explains the need for controls; it does not supply the complete corrections for a real gas-weighing instrument.

A positively charged three-membered nitrogen heterocycle. Intramolecular formation from a tertiary amino alcohol with an activated hydroxyl can be followed by regioselective nucleophilic ring opening and net ring expansion.

A neighbouring tertiary amine displaces a leaving group to form a three-membered ammonium ring; attack at the original ring carbon cleaves its old C–N bond and incorporates the side-chain carbon into an expanded nitrogen ring.

A backbone hydrogen bond is a hydrogen bond involving groups of the protein backbone, typically a backbone oxygen chemical atom and a hydrogen chemical atom already joined by a covalent bond to backbone nitrogen. It can connect positions that are not adjacent along the polypeptide chain. The peptide bonds still determine which amino acid residues are consecutive. See the original structural argument cited under alpha helix.

A beta sheet consists of extended stretches of protein backbone lying alongside one another, joined by backbone hydrogen bonds. The stretches can belong to different portions of the same polypeptide chain or to different chains.

Each extended stretch is a beta strand. Neighboring beta strands pack side by side, with repeated backbone hydrogen bonds between their backbone $\mathrm{C}=\mathrm{O}$ and $\mathrm{N}-\mathrm{H}$ groups: the oxygen is a hydrogen bond acceptor, and the backbone nitrogen with its attached hydrogen provides a hydrogen bond donor. These are interactions of the shared protein backbone, not merely contacts between amino acid side chains. Unlike an alpha helix, a beta sheet joins adjacent extended stretches rather than coiling one stretch around an axis. See Clark, Douglas and Choi, Biology 2e, 3.4: backbone groups in secondary structure.

Read each beta strand in the sequence direction from the N-terminus toward the C-terminus, even when it is an internal part of a longer polypeptide chain. In a parallel beta sheet, neighboring beta strands run in the same N→C direction; in an antiparallel beta sheet, they run in opposite N→C directions. A three-strand example can therefore have arrows right–right–right or right–left–right. A beta sheet can also mix the two arrangements. Direction does not identify chain membership: a single polypeptide chain can fold back to supply several beta strands, and different polypeptide chains can contribute to one beta sheet. See Alberts et al., Molecular Biology of the Cell: beta-sheet strand arrangements.

The pleated appearance comes from the geometry of the protein backbone. Successive amino acid residues carry amino acid side chains on alternating faces of an ideal beta strand, conventionally drawn above and below the sheet. The attachment positions are the amino acid alpha carbons. Thus a six-position cartoon has groups 1, 3 and 5 on one face and 2, 4 and 6 on the other. This alternation is a spatial pattern, not a rule that alternating positions must contain identical amino acids. See Clark, Douglas and Choi: side chains above and below the pleats.

Real beta sheets commonly twist and curve; pleating does not make them perfectly flat plates. Which beta strands are neighbors, how connecting regions join them, and how their faces pack are features of the three-dimensional protein structure. An alternating pattern in the protein primary structure alone neither establishes a beta sheet nor specifies a unique fold independently of surroundings and interacting molecules. See Breda et al., Protein Structure, Modelling and Applications: extended strands, sheet twist and three-dimensional organization and protein folding.

Why this arrangement is useful: repeated backbone hydrogen bonds organize extended chain regions into a framework that can contribute to the interior of a folded protein. Amino acid side chains and connecting loops give that framework chemical variety and can shape a protein binding site for a ligand. Its attractive feature is the combination of a reusable backbone pattern with variable exposed groups: similar beta sheets can support different recognition surfaces. See Alberts et al.: beta-sheet cores and loops that form binding sites.

Historically, Linus Pauling and Robert B. Corey published The Pleated Sheet, a New Layer Configuration of Polypeptide Chains in PNAS 37, 251–256 (1951). They reasoned from peptide bond geometry and possible backbone hydrogen bonds, proposing an idealized layer rather than measuring every modern beta sheet. Their initial model should not be identified with all present-day beta sheet geometries; they published further pleated-sheet configurations later in 1951. See Pauling and Corey: original 1951 paper and scan, ^[ref], and Pauling and Corey, Configurations of Polypeptide Chains With Favored Orientations Around Single Bonds: Two New Pleated Sheets, PNAS 37, 729–740 (1951).

Borazine is the alternating six-membered ${\mathrm{B}}_3{\mathrm{N}}_3{\mathrm{H}}_6$ ring. Planar boron and nitrogen centers permit N-to-B pi donation, but unequal orbital energies strongly polarize the bonding. It undergoes addition and hydrolysis much more readily than benzene; the structural analogy does not give benzene-like chemical inertness.

A carbamate contains the unit $\mathrm{O}-\mathrm{C}(\mathrm{O})-\mathrm{N}$. The nitrogen lone pair conjugates with the carbonyl; cyclic carbamates include 2-Oxazolidinone.

Walther Bothe and Herbert Becker observed penetrating radiation from beryllium struck by alpha particles before James Chadwick's interpretation.^[ref]

Irène Joliot-Curie and Frédéric Joliot found that adding material containing hydrogen increased ionization, interpreting the ejected protons as Compton scattering recoils from extremely energetic gamma rays. James Chadwick tested this interpretation against nuclear recoils in other elements.^[ref]

The counter coupled a small ionization chamber to an amplifier and oscillograph: charged particles produced ions, and the electrical signal gave a deflection. With Norman Feather, James Chadwick also observed nitrogen recoil tracks in a cloud chamber.^[ref]

The apparatus used polonium on silver facing beryllium inside an evacuable vessel. Paraffin wax before the aluminium counter window supplied recoil protons; intervening aluminium screens measured their particle range. Deflections were photographed on bromide paper. The first counter contained air; later fillings included hydrogen, helium, nitrogen, oxygen and argon. Counts with wax absent included gas recoils; wax insertion added entering protons. Thick lead between source and counter hardly changed the initial counts, testing penetration against the low background.^[ref]

The diagram separates two routes to a signal: a proton entering from the wax and a nuclear recoil created inside the chamber gas. Its lower row is a logical summary, rather than a reconstructed experimental trace. In either route the observed ionization belongs to a charged secondary particle; identifying the incident radiation requires an additional collision model.

In the February letter, a photon interpretation requiring about $52\mathrm{MeV}$ for the protons predicted only about $0.4\mathrm{MeV}$ for nitrogen recoils, below the observed ionization. Here $1\mathrm{MeV}=10^6$ electronvolts. James Chadwick proposed a neutral particle near the proton mass and the nuclear reactionThese are the letter's approximate historical values, not a modern mass determination.^[ref]

Why compare two materials? A gamma ray is a photon, so its incident momentum is $E_{\gamma }/c$, where $c$ is the speed of light. A slow massive projectile instead has momentum $mv$ and kinetic energy $m{v}^2/2$. The relationship between incoming momentum and energy therefore changes. An elastic collision model must explain the recoil endpoints for both target masses with the same incident projectile population. Calling the radiation neutral supplies no such agreement by itself.

The original measurements depended on particle range calibration, material in the path, detector response and whether a recoil was fully stopped in the sensitive gas. Large deflections alone need not specify a complete recoil energy. The calculations below expose the ideal collision assumptions behind the inference; applying them to a measured spectrum requires checking those assumptions.

The reservoir species $\mathrm{ClON}{\mathrm{O}}_2$, formed from ClO and NO2 with third-body stabilization. Heterogeneous reaction with hydrogen chloride can produce molecular chlorine and nitric acid, activating chlorine while removing reactive nitrogen from the gas phase. It belongs to the wider reactive nitrogen family, not to the narrow NO-plus-NO2 definition of NOx.