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millimolar 10 3 M kM kilomolar 10 −6 M μM micromolar 10 6 M MM megamolar 10 −9 M nM nanomolar 10 9 M GM gigamolar 10 −12 M pM picomolar 10 12 M TM teramolar 10 −15 M fM femtomolar 10 15 M PM petamolar 10 −18 M aM attomolar 10 18 M EM examolar 10 −21 M zM zeptomolar 10 21 M ZM zettamolar 10 −24 M yM yoctomolar 10 24 M YM yottamolar
Molar concentration or molarity is most commonly expressed in units of moles of solute per litre of solution. [1] For use in broader applications, it is defined as amount of substance of solute per unit volume of solution, or per unit volume available to the species, represented by lowercase : [2]
For example, the conversion of a flowrate of kg/s to kmol/s only requires dividing by the molar mass in g/mol (as = =) without multiplying by 1000 unless the basic SI unit of mol/s were to be used, which would otherwise require the molar mass to be converted to kg/mol.
In chemistry, the molar absorption coefficient or molar attenuation coefficient (ε) [1] is a measurement of how strongly a chemical species absorbs, and thereby attenuates, light at a given wavelength.
The term molality is formed in analogy to molarity which is the molar concentration of a solution. The earliest known use of the intensive property molality and of its adjectival unit, the now-deprecated molal, appears to have been published by G. N. Lewis and M. Randall in the 1923 publication of Thermodynamics and the Free Energies of Chemical Substances. [3]
The enzyme unit, or international unit for enzyme (symbol U, sometimes also IU) is a unit of enzyme's catalytic activity. [1]1 U (μmol/min) is defined as the amount of the enzyme that catalyzes the conversion of one micro mole of substrate per minute under the specified conditions of the assay method.
In chemistry, the mole fraction or molar fraction, also called mole proportion or molar proportion, is a quantity defined as the ratio between the amount of a constituent substance, n i (expressed in unit of moles, symbol mol), and the total amount of all constituents in a mixture, n tot (also expressed in moles): [1]
The smaller the dissociation constant, the more tightly bound the ligand is, or the higher the affinity between ligand and protein. For example, a ligand with a nanomolar (nM) dissociation constant binds more tightly to a particular protein than a ligand with a micromolar (μM) dissociation constant.