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A resonator stores oscillatory energy in one or more normal modes. Driving near a mode's frequency can produce resonance. Losses limit the response and determine its quality factor. After the drive is removed, an isolated weakly damped mode decays approximately exponentially; an observed room response may combine many modes.

Glycolysis converts glucose into two pyruvate molecules, with a net two ATP and reduced NADH; it does not directly consume molecular oxygen. Pyruvate processing and the citric acid cycle, also called the TCA cycle, release carbon dioxide and supply reduced carriers. Thus releasing carbon dioxide and consuming molecular oxygen occur at different stages.^[ref]

An electron transport chain reoxidizes carriers such as NADH. Coupling some of its redox steps to proton transport establishes an electrochemical gradient; ATP synthase can use that gradient to form ATP from adenosine diphosphate and inorganic phosphate. This is oxidative phosphorylation. A separate route, substrate-level phosphorylation, transfers a phosphate group from a reacting substrate to adenosine diphosphate. In typical eukaryotic biological cells, the respiratory chain occupies the inner membrane of a mitochondrion.^[ref]

The useful achievement is controlled transfer: fuel oxidation can replenish an ATP supply that supports active transport and synthesis. ATP is a reusable chemical carrier, not newly created energy; ATP hydrolysis and the coupled cellular process have their own net free energy balance. Some fuel energy is dissipated as heat.^[ref]

There is no universal yield of $36$ or $38$ ATP per glucose. Actual ATP recovery depends on carrier transfer routes, coupling and diversion of intermediates to other metabolism. In particular, an oxygen uptake rate cannot be converted into an ATP production rate by assuming one fixed multiplier.^[ref]

Reverberation is the persistence of acoustic waves after a source stops, produced by repeated reflections in an enclosure. A diffuse-room approximation gives an approximately exponential decay of mean acoustic energy; an individual normal mode may instead be described as a damped resonator.

The conventional reverberation time $T_{60}$ is the time for the level of decaying acoustic energy to decrease by $60$ decibels, a factor $10^6$ in energy or $10^3$ in pressure wave amplitude. For exponential energy decay $E(t)=E(0)e^{-t/{\tau }_E}$, $T_{60}=6\ln (10){\tau }_E$. It is not the exponential relaxation time itself and cannot be inferred exactly from an unspecified audibility threshold.

For shear ${\mathbf{u}}_0=-2Ax{\mathbf{e}}_y$, the spatially averaged perturbation kinetic energy obeys $dE/dt=2A\rho ⟨u_x^{\prime }{u}_y^{\prime }⟩-\rho \nu ⟨|\nabla {\mathbf{u}}^{\prime }{|}^2⟩$. Pressure and the Coriolis force do no net work. Thus positive radial-azimuthal velocity correlation extracts mean-flow energy. A leading two-dimensional shearing wave has $\mathrm{Re}(v_x{v}_y^{\ast })=-k_x{k}_y|Z{|}^2/k^4>0$.

// Target: astrophysics.bigb

A ribozyme is an RNA molecule whose folded structure provides catalysis of a chemical reaction. A protein enzyme builds its active site from an amino acid chain; a ribozyme builds a working active site from RNA, sometimes with metal ions and associated proteins. Base pairing can help recognize a substrate, but recognition alone does not establish catalysis: the RNA must promote chemical conversion. A passive messenger RNA template being read by a ribosome is not thereby a ribozyme. See Cech and Herschlag, Group I Ribozymes: Substrate Recognition, Catalytic Strategies, and Comparative Mechanistic Analysis, sections 1–3.

The surprise is that an information-bearing polymer can also perform chemistry. Examples include the self-splicing group I intron of Tetrahymena thermophila and the catalytic RNA component of bacterial RNase P, discussed below. The ribosome supplies an everyday example: its peptide bond-forming active site is made of ribosomal RNA, although the complete machine also contains proteins. Nissen and colleagues examined structures of a large ribosome subunit with substrate analogues and found RNA contacting those analogues at the catalytic centre. This supports an RNA active site, not a claim that isolated ribosomal RNA can carry out all of biological translation. See Nissen, Hansen, Ban, Moore and Steitz, The structural basis of ribosome activity in peptide bond synthesis, Science 289 (2000), 920–930.

For the Tetrahymena group I intron, RNA splicing removes the intron and joins its flanking exons. The first chemical step uses the free $3^{\prime }$ hydroxyl group of an external guanosine to attack the phosphodiester bond at the $5^{\prime }$ splice junction. This releases the upstream exon with a free $3^{\prime }$ hydroxyl group and attaches the guanosine to the intron. That newly freed hydroxyl group then attacks the phosphodiester bond at the other splice junction, joining the exons and releasing the linear intron. Each step exchanges one backbone connection for another; it is not simply separation of base pairs. See Cech, Zaug and Grabowski, 1981: the phosphoester-transfer mechanism.

The motivating experiment began with an unexpected control. As Cech recounts, Zaug purified a ribosomal RNA precursor from Tetrahymena using a detergent and phenol extraction, then compared test tubes with and without added cell nucleus extract. Incubation in salts and nucleotides released the same amount of small intron RNA in both cases, detected by gel electrophoresis. Repetition made a missing ingredient or accidental omission less plausible. Activity also survived treatments intended to destroy proteins. Nevertheless, absence of added extract did not by itself exclude a tightly attached, resistant protein, or prove that the small RNA had been newly excised rather than released from an already processed complex. See Thomas R. Cech, 1989 Nobel lecture, pp. 655–659: the unexpected control and alternative explanations.

An independent chemical readout addressed the latter problem. Cech mixed precursor RNA with phosphorus-32-labelled guanosine bearing three phosphate groups (GTP), and used gel electrophoresis followed by exposure to X-ray film to locate the label. Label appeared in the excised intron with magnesium present; it was absent when magnesium was omitted or labelled ATP replaced the labelled guanosine reagent. This experiment is described in Cech, 1989 Nobel lecture, pp. 657–658: labelled-guanosine controls. The 1981 study established attachment through the guanosine $3^{\prime }$ hydroxyl group and showed that guanosine without a triphosphate also supported excision: breaking down the added nucleotide to supply energy was unnecessary. See Cech, Zaug and Grabowski, In vitro splicing of the ribosomal RNA precursor of Tetrahymena, Cell 27 (1981), 487–496: primary abstract. Separately, sequencing and terminal analysis found an extra $5^{\prime }$ guanosine absent from the corresponding DNA sequence. See Zaug and Cech, The intervening sequence excised from the ribosomal RNA precursor of Tetrahymena contains a 5-terminal guanosine residue not encoded by the DNA, Nucleic Acids Research 10 (1982), 2823–2838. Together, incorporation and sequence evidence support a new covalent bond, beyond a change in how RNA associates.

Kruger, Grabowski, Zaug, Sands, Gottschling and Cech's 1982 test removed dependence on a precursor purified from Tetrahymena. They cloned the intron and adjacent exons into a DNA template, made precursor RNA with purified bacterial RNA polymerase under conditions suppressing RNA splicing, and removed proteins by detergent–phenol extraction. Denaturing gel electrophoresis separated precursor species. Purified precursor was then incubated with the guanosine reagent, magnesium and salt; matched samples without this incubation supplied a precursor baseline. Their standard assay used $10\mathrm{mM}$ magnesium chloride, $0.1\mathrm{mM}$ of that guanosine reagent, $100\mathrm{mM}$ ammonium sulfate and a buffer solution at pH $7.5$, for $30$ minutes at temperature $37{}^{\circ }\mathrm{C}$, with specified variations in individual experiments. Gel electrophoresis and radioactive-film detection showed excised intron RNA; sequencing verified its $5^{\prime }$ junction. See Kruger et al., Self-Splicing RNA, Cell 31 (1982), 147–157, figures 3–4 and Experimental Procedures.

Excision alone could leave disconnected exons. To test joining, the authors paired labelled RNA with DNA spanning the joined-exon sequence, removed exposed RNA with enzymes, and separated the protected pieces by denaturing gel electrophoresis. Spliced samples yielded protected RNA long enough to span the junction. See Kruger et al., 1982, figure 6: independent evidence for exon ligation. The experimental logic matters: an intron-sized band identifies a candidate product, while sequence and junction assays test its chemical identity.

These controls support sufficiency of the prepared RNA under the assay conditions. They do not show that every RNA self-splices, or that proteins are dispensable inside a biological cell. Many group I introns use proteins to help attain an active fold. See Cech and Herschlag, Group I Ribozymes, section 6: protein facilitation. Nor does a failed assay necessarily identify an inactive nucleotide sequence: unsuitable ions, pH, or temperature can prevent a working active site from forming.

The distinction between self-processing and repeated use became especially clear with bacterial RNase P. In 1983 Guerrier-Takada, Gardiner, Marsh, Pace and Altman separated the RNA and protein components of RNase P from two bacteria. Purified RNA cleaved precursor transfer RNA under conditions containing $60\mathrm{mM}$ magnesium ions, or $10\mathrm{mM}$ magnesium ions plus $1\mathrm{mM}$ spermidine. The protein components alone had no catalytic activity. At $5$–$10\mathrm{mM}$ magnesium without spermidine, both components were needed. Thus the comparison demonstrated an RNA catalyst while also explaining why protein assistance could matter under other conditions. RNase P produces the mature $5^{\prime }$ end of transfer RNA by removing its leader; it acts on a separate substrate and can be used again. See Guerrier-Takada et al., The RNA moiety of ribonuclease P is the catalytic subunit of the enzyme, Cell 35 (1983), 849–857: primary abstract.

Self-splicing demonstrates RNA chemistry, but one precursor completing one rearrangement is not yet evidence for catalytic turnover: repeated conversion of separate substrates by a regenerated catalyst. The self-splicing precursor changes its own connectivity and incorporates external guanosine. In 1986 Zaug and Cech showed that a shortened Tetrahymena intron RNA could cleave and rejoin separate short RNA substrates in a sequence-dependent reaction. This demonstrated an RNA enzyme acting beyond its own self-processing. See Zaug and Cech, The intervening sequence RNA of Tetrahymena is an enzyme, Science 231 (1986), 470–475: primary abstract.

Read the second figure as a counting argument. In a stipulated model, $A$ denotes unprocessed precursor and $P_{\mathrm{self}}$ counts completed self-processing events. Set $A(0)=R_0$, $P_{\mathrm{self}}(0)=0$ and $dA/d\tau =-A$. The exponential function solution gives $P_{\mathrm{self}}/R_0=1-e^{-\tau }$, never exceeding one. Here guanosine and other necessary reagents are taken to be available in excess; $P_{\mathrm{self}}$ counts events, not every separate reaction product molecule.

For a second stipulated model, let an unchanged ribozyme $R$ perform $R+S⟶R+P$ on a separate substrate $S$. Assume the effective law of mass action $dS/dt=-kRS$, no reverse reaction, no ribozyme loss and no inhibited or long-lived bound states. Set $R=R_0$, $S(0)=5R_0$, $P(0)=0$ and $\tau =k{R}_{0}t$. Then $S/R_0=5e^{-\tau }$ and $P/R_0=5(1-e^{-\tau })$, with $S+P=5R_0$. At $\tau =1$, self-processing gives about $0.632$ completed events per initial RNA, whereas the regenerated ribozyme gives about $3.161$ reaction product molecules per initial ribozyme. More than one substrate conversion per initial ribozyme, with appropriate background and identity controls, is evidence for turnover. Product accumulation below that threshold alone cannot distinguish a reusable catalyst from one-shot chemistry. These models illustrate that distinction; actual enzyme kinetics can include folding delays, binding, saturation and product release.

Richard Arnowitt co-developed a canonical treatment of general relativity with Stanley Deser and Charles W. Misner. Their framework organizes spatial geometry, conjugate momenta and constraints, and supplies an asymptotic definition of gravitational energy.^[ref]

The Arnowitt-Deser-Misner energy is associated with suitable asymptotic boundary conditions; it is not a universal pointwise energy-density formula for an arbitrary spacetime.

For a photon and a massive particle with zero total momentum, their momenta are opposite and equal. Conservation of total energy fixes the same momentum magnitude before and after elastic scattering, independently of direction. A right-angle photon turn therefore makes the recoiling particle move perpendicular to the original photon direction in that frame. Transform both velocity components, or the complete four-momentum, to obtain the laboratory recoil; a transverse component is reduced by the boost Lorentz factor when the particle has zero longitudinal velocity in the zero-momentum frame.

If $A(t)$ and $B(t)$ are perpendicular four-dimensional spatial vectors of equal fixed magnitude, every constant-time slice is a planar circle. Opposite rotations in two orthogonal coordinate planes can produce a Nambu–Goto action solution with constant radius and a rotating plane. The induced worldsheet metric can be constant even though the embedding moves. Rotating Cartesian axes clarify its shape without removing its kinetic target-space energy.

For unstressed central Hookean springs, the quadratic elastic energy is $\frac{1}{2}{\sum }_{ij}{k}_{ij}[{\mathbf{n}}_{ij}\cdot ({\mathbf{u}}_i-{\mathbf{u}}_j){]}^2$, with unit edge direction ${\mathbf{n}}_{ij}$. A common translation gives zero displacement difference. An infinitesimal rotation ${\mathbf{u}}_i=\mathbf{\Omega }\times {\mathbf{r}}_i$ also gives zero extension because a vector is perpendicular to its cross product with $\mathbf{\Omega }$. Thus a noncollinear three-dimensional free framework has three translational and three rotational zero modes. Extra mechanisms can give additional zero modes; six is a lower bound until rigidity is established.

Ringdown is the freely decaying motion of a resonator after an applied drive is removed. For an underdamped damped harmonic oscillator, the amplitude decays as $e^{-\gamma t}$ while the angular frequency is $\nu =\sqrt{{\Omega }^2-{\gamma }^2}$. In the weak-damping limit, the cycle-averaged stored energy decays as $e^{-2\gamma t}$, giving the quality factor from ringdown $Q\simeq \Omega /(2\gamma )$.

For two weakly damped normal modes with initial intensity ratio $R_0>1$, independent exponential energy decay gives $I_1(t)/I_2(t)=R_0{e}^{-t({\omega }_1/Q_1-{\omega }_2/Q_2)}$. An observed reversal to a ratio below one implies the displayed upper bound on $Q_1$, provided the denominator is positive. A strict intensity comparison does not determine a unique quality factor; equality fixes only the crossing threshold.

An RLC circuit combines electrical resistance $R$, inductance $L$, and capacitance $C$. The capacitor stores energy in its electric field; the inductor stores energy in its magnetic field. Their exchange can produce an oscillation, while Joule heating removes energy. A series RLC circuit gives a particularly clear example: changing $R$ turns ringing into a direct return to equilibrium, and changing $L$ or $C$ tunes a resonance.

These circuits connect two useful viewpoints. In time, they describe how stored energy is released after switching. In frequency, they select a range of signals: the resonant series RLC response explains radio tuning and simple filters. The same mathematics describes a damped harmonic oscillator, so insight about mechanical ringing transfers directly to an electrical circuit. ^[ref]; ^[ref].

An RL circuit combines electrical resistance $R$ and self-inductance $L$. In the series model, the same electric current $I$ flows through both components. An ideal battery maintains terminal electric potential difference $V$; the drops in the direction of positive electric current obey Ohm's law and the inductor relation:This is Kirchhoff's voltage law with the inductor's terminal drop, rather than its oppositely signed induced electromotive force. For constant $R>0$, $L>0$, and $V$, the first-order linear differential equation has solutionThe time constant $\tau$ measures exponential decay of the difference from the final electric current. ^[ref].

For a stipulated example, take electrical resistance $R=2\Omega$, self-inductance $L=0.5\mathrm{H}$, terminal electric potential difference $V=6\mathrm{V}$, and initial electric current $I(0)=0$. ThenWith $t$ measured numerically in seconds, this is $I(t)=3(1-e^{-4t})$ in amperes. At one time constant,and the terminal electric potential difference drops areTheir sum is exactly $6\mathrm{V}$. At $t=0^{+}$, the inductor takes the entire terminal electric potential difference while the electric current is still zero. At steady electric current, the inductor's terminal drop is zero and the entire drop is across the electrical resistance.

The final magnetic energy stored by the inductor is $U_{\infty }=L{I}_{\infty }^2/2=2.25\mathrm{J}$. At one time constant, the electric current has reached about $63.21\%$ of its final value, but its magnetic energy has reached only about $39.96\%$:This difference follows from the square of electric current in the inductor's magnetic energy.

For release, take $t=0$ at the start of a separate experiment with initial electric current $3\mathrm{A}$. Remove the battery from the model while maintaining a closed path through the same electrical resistance and inductor. ThenNow $v_L=-v_R$: the induced electromotive force supports the continuing positive electric current as its magnitude decreases. This closed-loop model describes exponential decay, not opening the sole path and imposing an instantaneous jump to zero electric current. The inductor's magnetic energy and the power of Joule heating areTheir time constant is $\tau /2=0.125\mathrm{s}$. The total energy dissipated by Joule heating is exactly the initial magnetic energy:The second diagram in inductor shows this energy transfer. A finite closed path lets us predict both how long the electric current persists and how much energy becomes heat. ^[ref].

An experimental atomic physicist who, with Willis Eugene Lamb Jr., measured the Lamb shift in 1947. Their microwave method distinguished hydrogen levels that the simplest relativistic theory placed at the same energy. The experiment made a small spectral discrepancy into a precise test, helping motivate improved calculations in quantum electrodynamics.^[ref]

Robert R. Wilson proposed using fast protons for radiation therapy by exploiting their depth-dependent energy deposition. A proton loses kinetic energy along its path and has enhanced stopping near the end of its range, producing a Bragg peak. His 1946 paper connected this measured interaction with a way to concentrate irradiation at a chosen depth. The physical idea links particle accelerator design, stopping power and spatial control of deposited energy.^[ref]

Physicist who proposed the use of fast protons for radiation therapy in 1946.^[ref]

Wilhelm Conrad Röntgen's 1895 first communication describes an induction coil driving an evacuated gas-discharge tube, enclosed in black cardboard in darkness. A paper screen coated with barium platinocyanide showed fluorescence even with its uncoated side facing the tube, visible two metres away. The covering excluded ordinary illumination.^[ref]

He interposed materials: a thousand-page book transmitted; $1.5\mathrm{mm}$ lead was practically opaque. A stepped stack of foil produced a photographic plate record. Different materials were not equivalent at equal density and thickness. Photographic plates checked visual observations while remaining covered against ordinary illumination.^[ref]

Section 14 lists photographs of hand bones, wire on a bobbin, boxed weights, an enclosed compass, and a lead-painted door. It does not identify the hand's owner. Magnetic deflection moved the cathode ray impact point and thus the source, without bending the emerging X-rays. Their nature remained unsettled.^[ref]

The observations belong to 1895; the contemporary English translation appeared in Nature on 23 January 1896.^[ref] The experimental logic separates production, transmission and detection. A visibly opaque covering can transmit X-rays; fluorescence then converts deposited energy into visible light. A shadow measures a difference between paths through an object, rather than a direct view of its surface. Neither a screen's brightness nor photographic darkness alone measures an absolute X-ray energy or establishes the X-ray attenuation law below.

Rory Hulse coauthored An atomistic modelling study of the properties of dislocation loops in zirconium by Rory Hulse and Christopher P. Race. The work constructs and relaxes atomistic models of dislocation loops in zirconium, comparing their energies, shapes and orientations. Such comparisons help connect microscopic defects with irradiation growth in a structural material.^[ref]

The Yanai wave is the $n=0$ branch of the equatorial shallow-water dispersion relation with positive frequency:Its group velocity is $d\omega /dk=c{\omega }^2/({\omega }^2+\beta c)>0$. At low frequency it has westward phase velocity but transports energy eastward; at high frequency its phase and group velocities approach $c$.

A wave packet can transfer energy downstream faster than individual phase features move, allowing successive downstream disturbances to develop while upstream ones weaken. In the simple uniform-current barotropic model with zero meridional wavenumber, the zonal group speed is $U+\beta /k^2$ while phase speed is $U-\beta /k^2$. Linear superposition and interference are not direct nonlinear eddy scattering. Real weather development also involves baroclinic energy conversion and wave–mean-flow feedback, which require additional dynamics.