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Absorption takes a chemical substance into a material's bulk, as when carbon dioxide dissolves in water. Adsorption instead concerns accumulation at a boundary. Bulk uptake and interfacial accumulation can coexist; total uptake alone does not separate their contributions. This use of absorption concerns material uptake, whereas absorbance describes attenuation of electromagnetic radiation.

Conversion of an acetal and water to its corresponding carbonyl compound and alcohols.

Acetic acid is a weak acid that partly transfers protons to water, supplying hydronium and negative ions. It is therefore a weak electrolyte in water.

Acetone reacts with iodine to form iodoacetone, iodide, and a hydrogen ion:In water, ${\mathrm{H}}^{+}$ denotes a solvated hydrogen ion; added hydrochloric acid provides acidic conditions.

Moorpark College's protocol mixes acetone, hydrochloric acid and water from burets in matched test tubes; pipet in iodine, swirl and time colour loss against white paper. Use water, then reacted solution, as references. Duplicate each mixture; keep total volume $5.00\mathrm{mL}$ and run temperatures within $2{}^{\circ }\mathrm{C}$.^[ref]

The stock dilutions give $[\mathrm{acetone}{]}_0=0.800$, $[{\mathrm{H}}^{+}{]}_0=0.200$, and $[{\mathrm{I}}_2{]}_0=0.00100\mathrm{mol}{\mathrm{L}}^{-1}$. B and C separately double acetone and acid; D halves iodine. The manual supplies no measured times; it states zero partial order of reaction in iodine and asks students to determine the other exponents.^[ref]

The endpoint measurement is a time $\tau$ to an operational colour threshold, not direct observation of a reaction intermediate. If the iodine disappearance rate $r$ is approximately constant until that endpoint, $r\approx [{\mathrm{I}}_2{]}_0/\tau$. Halving $[{\mathrm{I}}_2{]}_0$ at fixed other concentrations then approximately halves $\tau$ without changing $r$. A longer or shorter endpoint time alone is not a comparison of reaction rates unless the starting concentration is included. For an observed power-form rate law, doubling only acetone gives a rate ratio $2^m$ and hence $m=\ln (r_B/r_A)/\ln 2$; doubling only acid similarly estimates its own partial order of reaction. Those are inference formulas, not asserted experimental results.

A useful proposed reaction mechanism would explain how iodine is consumed after an earlier transformation sets the throughput, making the observed reaction rate insensitive to iodine over a tested range. The observed zero exponent would contradict treating this net chemical equation as a single elementary reaction with directional rate law $k[\mathrm{acetone}][{\mathrm{I}}_2]$. It would not uniquely prove which reaction intermediate or earlier step is involved. Independently detecting a candidate reaction intermediate would provide another kind of evidence.

The excess-reactant approximation has an explicit scale: the baseline iodine inventory is only $0.00100/0.800=0.125\%$ of the initial acetone inventory, and its net hydrogen ion production is $0.00100/0.200=0.5\%$ of the initial acid inventory, assuming only the stated one-to-one chemical reaction. These are calculated bounds on composition change, not measured reaction orders. Mixing delay, a subjective colour threshold, and temperature drift limit the inference. Repeats and a fixed viewing geometry help; a calibrated absorbance trace could test linearity during conversion instead of relying on an endpoint alone. That extension would require a reference blank and a justified Beer-Lambert law calibration, rather than treating visible colour as an exact concentration. A zero-order reaction approximation in iodine must fail at depletion; it cannot imply consumption after no iodine remains.

Acid-base chemistry studies how chemical acids and chemical bases exchange protons or electron pairs. Here the focus is transfer of protons in water: a chemical acid donates a proton, and a chemical base accepts it. The resulting chemical equilibrium determines pH, while a buffer solution can resist changes in pH. This connects microscopic chemical reactions with a compact, measurable description of a chemical solution.

The important distinction is between how much chemical acid is present and how readily it transfers a proton. A weak acid and a strong acid at the same total concentration need not have the same pH. Conversely, two buffer solutions can have the same pH while containing very different total quantities of their chemical acids and chemical bases.

The institutional experiment The Potentiometric Titration of an Acid Mixture, from Massachusetts Institute of Technology's 5.310 Laboratory Chemistry, determines hydrochloric acid and phosphoric acid inventories. Dried potassium hydrogen phthalate standardizes sodium hydroxide. A volumetric pipette selects an acid aliquot, diluted with water in a beaker. A burette feeds a stirred sample beside a glass electrode; the apparatus isolates the sample from stirrer warming. The burette is conditioned with titrant and its tip freed of bubbles. Stable pH and added volume are recorded, with smaller additions near the transition. Controls include replicate standardizations, a consistent pale-pink phenolphthalein endpoint, and a standard buffer solution check between sample runs. The readout supports inventory estimates through known stoichiometry; it does not directly count molecules.^[ref]

The same protocol requires drainage time for burette readings and warns that an undelivered hanging drop spoils the association between volume and pH. Its color-persistence wording differs between the main paragraph and footnote, so a reproducible titration endpoint needs an explicitly chosen criterion. Its acid mixture is not the single-strong acid ideal model above.^[ref]

A distinct control appears in Process Measurement Procedures: Sulfuric Acid Emissions, §1.4.4.2: the phenolphthalein standardization is repeated with water replacing the acid, matching the sample aliquot and indicator quantity. The volume needed for the same pink endpoint is subtracted from the sample reading.^[ref]

The independent bookkeeping for such a matched blank is $n_A=c_B(V_{\mathrm{sample}}-V_{\mathrm{blank}})$, assuming one-to-one neutralization and equal background consumption. A blank cannot correct an unmatched chemical reaction or guarantee exact coincidence of endpoint and equivalence point. Subtracting pH readings would not give this inventory correction, because pH is a logarithm. Repeatability constrains scatter; an independently known check sample also tests systematic bias. Carbon dioxide uptake, incomplete mixing, electrode drift, and uncertain titrant concentration limit the inference.

The acid dissociation constant quantifies the chemical equilibrium for loss of one proton from a chemical acid. In water, write the actual proton transfer as $\mathrm{HA}+{\mathrm{H}}_2\mathrm{O}\rightleftharpoons {\mathrm{H}}_3{\mathrm{O}}^{+}+{\mathrm{A}}^{-}$. Its full dimensionless equilibrium constant isThe usual aqueous acid dissociation constant uses the solvent convention with water thermodynamic activity approximated by one:Here hydrated hydrogen ions are understood; ${\mathrm{H}}^{+}$ is shorthand, not an isolated bare proton in the chemical solution. All thermodynamic activities and $K_a$ are dimensionless quantities, using consistent standard states. If water thermodynamic activity differs appreciably from one, retain it in the full equilibrium constant instead of silently mixing conventions.

With activity coefficients ${\gamma }_i$ and reference concentration $c^{\circ }=1\mathrm{mol}{\mathrm{L}}^{-1}$, put $a_i={\gamma }_i[i]/c^{\circ }$ for each solute. ThenThe last expression is the dilute ideal concentration approximation, not the definition in a nonideal chemical solution. Omitting $c^{\circ }$ instead produces a quotient with units of concentration; its numerical value depends on the chosen units. Do not take a logarithm of that dimensional quotient. Conditional concentration quotients can change with ionic strength even at fixed temperature, whereas the thermodynamic acid dissociation constant retains the activity coefficient corrections. The acid dissociation constant entry distinguishes these conventions.

At the same temperature, solvent and standard states, a larger acid dissociation constant, equivalently a smaller pKa, indicates a stronger tendency to donate a proton. It does not specify an analytical concentration, a pH, or a reaction rate. Composition and the weak acid mass and charge balances are needed to predict pH; chemical kinetics addresses how quickly the chemical equilibrium is approached.

An increase in oxidation state records oxidation; a decrease records reduction. Thus ${\mathrm{Fe}}^{2+}\to {\mathrm{Fe}}^{3+}$ raises the iron oxidation state by one, while ${\mathrm{MnO}}_4^{-}\to {\mathrm{Mn}}^{2+}$ lowers the manganese oxidation state from $+7$ to $+2$. Five iron ions supply the five-electron inventory required per permanganate ion.

In an acidic chemical solution, the complete half-reactions areFirst balance oxygen with four water molecules, then hydrogen with eight protons, and finally electric charge with five electrons. Multiply the iron half-reaction by five and add; the exchanged electrons cancel:Both sides contain one manganese, four oxygen, eight hydrogen and five iron chemical atoms, with net electric charge $+17e$. The ${\mathrm{H}}^{+}$ notation represents the acidic aqueous proton inventory; it does not imply bare protons moving independently of water. These half-reactions and their sum are the acidic balance used in the documented permanganate-iron titration.^[ref]

The coefficients predict amounts consumed, not a collision of five ions or an elementary reaction. Bulk chemical solution also contains compensating counterions, which are omitted from this net chemical equation. The hydrogen and oxygen oxidation states are unchanged; balancing their inventories remains essential even though they do not account for the exchanged electrons.

Adenosine deaminase catalyzes conversion of adenosine and water into inosine and ammonia. Its zinc-containing active site activates water and stabilizes the reacting configuration; proton transfers assist addition and leaving-group departure. Mutation kinetics constrain catalytic roles but do not uniquely locate every proton.

ATP is a nucleotide consisting of adenosine, itself adenine joined to ribose, carrying three phosphate groups. From the ribose outward, these groups are labelled $\alpha$, $\beta$, and $\gamma$. ATP connects energy-supplying processes to energy coupling for synthesis and active transport; the same carrier can be regenerated and reused. ^[ref].

The net hydrolysis commonly used in energy coupling isHere ${\mathrm{P}}_i$ denotes inorganic phosphate. At buffered pH $7$, this biochemical shorthand groups the appropriate protonation states into pools and leaves proton exchange with the buffer solution implicit. An explicit, charge-balanced choice is ${\mathrm{ATP}}^{4-}+{\mathrm{H}}_2\mathrm{O}⟶{\mathrm{ADP}}^{3-}+{\mathrm{HP}{\mathrm{O}}_4}^{2-}+{\mathrm{H}}^{+}$, without implying these are the only chemical species present. See the IUBMB recommendations for biochemical thermodynamics.

The quoted textbook biochemical standard state value is approximatelyThis convention uses fixed pH $7$, temperature $298.15\mathrm{K}$ ($25{}^{\circ }\mathrm{C}$), reference pressure $100\mathrm{kPa}$ ($1\mathrm{bar}$), unit reference thermodynamic activities for dissolved reactants and reaction products, and water thermodynamic activity approximated by one. The prime indicates the fixed-pH biochemical convention. See OpenStax Biology 2e, 6.4: standard ATP hydrolysis value and Biology 2e, 6.2: biochemical standard conditions. This is a reference value, rather than a universal value inside a biological cell; precise tables must also specify chemical solution conditions and any magnesium ion binding convention. Different reference conventions and data treatments give different tabulated values, as discussed in Li et al., 2010: a database of thermodynamic quantities for biochemical reactions.

An exergonic reaction has a negative change in Gibbs free energy, so the overall ATP hydrolysis is favourable under those reference conditions. Breaking a chemical bond by itself costs energy; forming new chemical bonds can release energy. The net change compares all reactants with all reaction products, including their interactions with water and the entropy contribution. Calling the phosphate connection a "high-energy bond" describes a large favourable change in Gibbs free energy on hydrolysis, rather than energy released by bond breaking alone. See 7.5 Strengths of Ionic and Covalent Bonds and Cooper, The Cell: ATP and metabolic energy.

Composition changes the driving force. At the same fixed pH, temperature, pressure, and binding convention, write the molar reaction change asHere $R$ is the molar gas constant, $T$ the absolute temperature, and $a$ a dimensionless thermodynamic activity for a biochemical pool. Constant water thermodynamic activity is absorbed into the reference term; fixed pH accounts for buffered protons. The shorthand $\Delta G$ means transformed molar reaction Gibbs free energy change, ${\Delta }_r{G}^{\prime }$, rather than a finite sample's total change. The natural logarithm acts on a dimensionless reaction quotient, never on concentrations with units. See the IUBMB biochemical thermodynamics recommendations and the general equilibrium constant relation.

For a stipulated ideal dilute chemical solution, let $a_i=[i]/c^{\circ }$, with $c^{\circ }=1\mathrm{mol}{\mathrm{L}}^{-1}$. Choose $[\mathrm{ATP}]=5\mathrm{mmol}{\mathrm{L}}^{-1}$, $[\mathrm{ADP}]=0.5\mathrm{mmol}{\mathrm{L}}^{-1}$, and $[{\mathrm{P}}_i]=1\mathrm{mmol}{\mathrm{L}}^{-1}$, ignoring activity coefficient corrections and magnesium binding. These are illustrative inputs, not a claim about a particular biological cell. ThenandIncreasing $Q$ tenfold raises $\Delta G$ by $RT\ln 10\approx 5.708\mathrm{kJ}\mathrm{mo}{\mathrm{l}}^{-1}$ at this temperature. Thus the ATP to ADP ratio and available inorganic phosphate matter, even with the same standard state value. These are local molar predictions at the stipulated composition, rather than a constant total yield as an isolated sample reacts.

Aerobic respiration uses molecular oxygen as the final electron acceptor. For complete oxidation of glucose, the net material balance isThis records the overall conversion of glucose, molecular oxygen, carbon dioxide and water; it is not one enzyme-catalyzed step, and it omits the separate ATP accounting. For an original stoichiometry check, each side contains six carbon, twelve hydrogen and eighteen oxygen chemical atoms. If exactly $1\mathrm{mmol}$ of glucose undergoes this complete conversion, the equation requires $6\mathrm{mmol}$ of molecular oxygen and yields $6\mathrm{mmol}$ each of carbon dioxide and net water. This is an equation-based calculation, not an observed seed measurement.

The molecular oxygen is reduced to water, rather than being the source of the carbon dioxide's carbon. A formal redox electron balance, using acidic half-reaction notation, makes the roles explicit:Adding and cancelling gives the net equation above. Both half-reactions conserve chemical atoms and electric charge. The $24$ electrons balance a net transfer; they are carried through cellular intermediates, rather than released as a pool of free electrons. The final respiratory reduction can be written ${\mathrm{O}}_2+4{\mathrm{H}}^{+}+4e^{-}⟶2{\mathrm{H}}_2\mathrm{O}$. These equations are bookkeeping, not a tracing experiment that assigns every product oxygen chemical atom to its original molecule.^[ref]

A change in cloud microphysics or cloud properties caused by aerosol, including droplet activation, precipitation changes and adjustments of water content or coverage. The Twomey effect isolates a fixed-water-content optical response; it does not by itself establish the sign or magnitude of every cloud adjustment.

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]

Amount of substance measures a count of specified entities, such as chemical atoms, molecules, ions, or electrons, using the mole as its SI base unit. It differs from mass: equal amounts of substance of different chemical substances contain equal entity counts but generally have different masses. If $N$ entities are present, $n=N/N_{\mathrm{A}}$, where $N_{\mathrm{A}}$ is the Avogadro constant. The specified entity matters: one mole of water molecules contains two moles of hydrogen chemical atoms. ^[ref]

An amphiphile is a molecule containing distinct hydrophilic and hydrophobic regions. Amphiphilic and amphipathic describe this combination. Membrane-forming phospholipids are examples; their two regions give different parts of one molecule different affinities for water. The word describes a structure, not a guarantee of a particular aggregate shape. See IUPAC Gold Book: amphiphilic.

The Anderson positron track experiment identified a light positively charged particle, now called the Positron, by combining magnetic bending, loss of kinetic energy in lead, and particle range. Each observation answered a different question: bending constrained momentum, the lead supplied a direction of travel, and particle range tested the proposed mass.

Carl David Anderson's The Positive Electron (1933), pp. 491–493, describes the 1932 discovery in a vertical cloud chamber with a $15,000\mathrm{gauss}$ magnetic field. A $6\mathrm{mm}$ lead plate separated two photographed track segments. The effective viewing depth was $1\mathrm{cm}$ along the magnetic field, with $14\mathrm{cm}$ transverse diameter: this restricted out-of-plane motion. The photographic readout supplied curvature on both sides. Comparisons with electron tracks under the same conditions constrained ionization; specific ionization was not directly measured for these events. He tested accidental alignment of unrelated tracks and rejected a reversed electron interpretation requiring an increase of kinetic energy in lead. Assuming unit electric charge, the mass bound was about twenty electron masses, rather than an exact mass determination. The paper credits Robert Andrews Millikan with the design and Seth Henry Neddermeyer with assistance.^[ref]

Preparation used rapid piston expansion and a water–alcohol mixture in the cloud chamber; cooling permitted droplets to form along ionization trails. A camera photographed these droplets. Initially, expansions occurred at random, so many photographs contained no tracks. Later counter triggering improved the useful yield.^[ref]

In The Production and Properties of Positrons, his 1936 lecture, Carl David Anderson describes the chamber inside an electromagnet and explains why the lead plate was decisive: after losing kinetic energy, a particle bent more sharply. He describes a proton hypothesis predicting only $5\mathrm{mm}$ of particle range, against an observed path longer than $50\mathrm{mm}$. These are historical values from the lecture, not the stipulated example below. The point was the incompatibility of particle range with the momentum inferred from curvature, rather than positive electric charge alone.^[ref]

The 1869 The Bakerian Lecture: On the Continuity of the Gaseous and Liquid States of Matter by Thomas Andrews describes dried carbon dioxide trapped above mercury in a sealed capillary tube. A steel screw pressurized water in a strong copper tube; movable mercury transmitted the load. A second capillary tube held air as a pressure gauge. Flowing water around the visible capillary tubes controlled temperature; a thermometer read the bath. A cathetometer read column positions, converted to volume readings using weighed-mercury calibration.^[ref]

Below the critical temperature, compression produced a visible liquid–gas boundary; above it, large density changes occurred without that boundary. Three trials gave $30.92{}^{\circ }\mathrm{C}$ as his critical temperature. Purity checks detected residual air; mercury height corrections accounted for unequal hydrostatic pressures. He explicitly left air nonideality and pressure-induced tube-capacity corrections unresolved, so his air-gauge pressures were approximate. These readouts support a liquid-gas critical point; they do not measure a homogeneous unstable loop or establish universal quantitative accuracy of the later Van der Waals equation.^[ref]

A disappearing liquid meniscus by itself has more than one possible explanation: in ordinary subcritical condensation or evaporation, one thermodynamic phase can simply run out. The stronger critical-point inference combines temperature control, compression readings and the existence of a continuous route around the endpoint of the phase coexistence curve. On that route a dilute gas can become dense without crossing a two-phase boundary. This is what continuity of liquid and gas means; it does not remove their distinct equilibrium number densities below $T_c$.

In his 12 December 1910 Nobel lecture, Johannes Diderik van der Waals explained gases and liquids through the same moving molecules, with attraction and finite size modifying their pressure. He also rejected the idea that constant $a,b$ should give universal numerical agreement. His critical-volume discussion explicitly retained derivatives of a volume-dependent $b$: the familiar $v_c=3b$ follows only when those derivatives are neglected. Thus the elegant constant-parameter Van der Waals critical point is a model result whose limitations were already part of its author's account.^[ref]

Anoxygenic photosynthesis captures light without producing molecular oxygen. It occurs in some bacteria and uses electron sources other than water. Whether carbon fixation accompanies this light capture depends on the organism and conditions; photosynthesis does not imply one universal carbon-assimilation pathway. See Alberts et al.: chloroplasts and photosynthetic bacteria.

A submerged object looks shallower because its emerging light rays bend away from the surface normal vector. Their backward extensions give an approximate virtual image nearer the surface. For an object at perpendicular depth $d$ in a medium of refractive index $n_{\mathrm{obj}}$, viewed through a flat boundary from a medium of refractive index $n_{\mathrm{obs}}$, the near-normal paraxial approximation gives $d_{\mathrm{par}}=(n_{\mathrm{obs}}/n_{\mathrm{obj}})d$. Thus the model water depth $12\mathrm{cm}$ appears approximately $9\mathrm{cm}$ from air. This is a bundle-of-light rays statement, not a deflection of the axial light ray.^[ref]

For general transmitted light rays, specify what “depth” means. Put the object at $(0,-d)$ below a horizontal boundary $z=0$. A light ray reaches the boundary at $(x,0)$, with object-side angle ${\theta }_{\mathrm{obj}}$ and observer-side angle ${\theta }_{\mathrm{obs}}$, both measured from the upward normal vector. For $x>0$, its backward extension meets the object's normal line $x=0$ at $z=-d_{\mathrm{axis}}$, whereThis axis-intercept depth is exact for that one transmitted light ray in the stated model. It tends to $d_{\mathrm{par}}$ as the angles tend to zero; at exactly zero the quotient is interpreted as a limit. These elementary tangent, sine and cosine relations show precisely where the small-angle approximation enters.

The original calculations below use $d=12\mathrm{cm}$, $n_{\mathrm{obj}}=4/3$ and $n_{\mathrm{obs}}=1$:

At appreciable obliquity these depths differ, so the full outgoing bundle has no single exact virtual image on the object's normal line. An oblique eye samples a narrow bundle; its local apparent position also depends on that bundle and cannot be inferred by declaring $d_{\mathrm{axis}}$ to be a universal image depth. A plane refracting boundary gives approximate image formation near normal incidence, with departures at larger angles. The construction assumes a flat surface, uniform transparent media with isotropy, and a propagating transmitted light ray; it does not extend to total internal reflection.

Archimedes' principle states that buoyancy equals the downward gravitational weight, or weight, of the displaced fluid. In a resting fluid of constant mass density ${\rho }_f$ under uniform gravitational acceleration $g$, its magnitude isHere $V_{\mathrm{displaced}}$ is the volume from which the body excludes the fluid: the whole external volume for a fully immersed solid body, and just the immersed volume for a partly immersed one. The body's own mass does not enter this buoyancy formula. ^[ref]

A short proof outline for a fully immersed body is to imagine replacing it by exactly the fluid it displaces. The surrounding hydrostatic pressure is unchanged. That replacement fluid is at rest, so its upward pressure force must balance its downward force from gravity. The original body receives the same inward pressure forces on the same closed surface, hence the same upward buoyancy.

Equivalently, let $\Omega$ be the displaced region, $\partial \Omega$ its closed surface and ${\mathbf{e}}_z$ the upward unit direction. The divergence theorem, applied component by component to the surface integral, and hydrostatic pressure giveThis also explains why horizontal forces cancel even for an irregular shape. A spatially constant surface pressure contributes zero to the closed-surface integral. If the mass density varies with depth, replace ${\rho }_f{V}_{\mathrm{displaced}}$ by the mass ${\int }_{\Omega }{\rho }_{f}dV$ of the displaced fluid.

The closed-surface argument assumes that the fluid applies pressure over the entire boundary of a fully immersed body. A body sealing against a tank bottom may have no fluid beneath it; then the lower-face pressure force used in the proof is absent, and a supporting contact force must be treated separately. For partial immersion, the usual buoyancy formula assumes the exposed surface receives the common atmospheric pressure, neglects the much smaller buoyancy from the air, and neglects surface tension.

For the $0.10\mathrm{m}$ cube in the stipulated water, full immersion displaces $0.001{\mathrm{m}}^3$, so $F_b=1000\times 9.81\times 0.001=9.81\mathrm{N}$. If its uniform mass density is $600\mathrm{kg}{\mathrm{m}}^{-3}$, its mass is $m=600\times 0.001=0.600\mathrm{kg}$ and its downward force from gravity is $mg=5.886\mathrm{N}$. To hold it fully immersed at rest requires an additional downward forceOn release from rest it initially moves upward; its eventual floating equilibrium has a smaller displaced volume. A same-size cube of uniform mass density $1200\mathrm{kg}{\mathrm{m}}^{-3}$ has mass $1.200\mathrm{kg}$ and downward force from gravity $11.772\mathrm{N}$. Full immersion still gives $9.81\mathrm{N}$ of buoyancy, leaving an initial net downward force of $11.772-9.81=1.962\mathrm{N}$. Subsequent motion also involves drag.