The alpha carbon in organic chemistry refers to the first carbon that attaches to a functional group (the carbon is attached at the first, or alpha, position). By extension, the second carbon is the beta carbon, and so on.
This nomenclature can also be applied to the hydrogen atoms attached to the carbons. A hydrogen attached to an alpha carbon is called an alpha-hydrogen (α-hydrogen), a hydrogen on the beta-carbon is a beta-hydrogen, and so on.
This naming standard is sometimes considered to be not in compliance with IUPAC nomenclature (which encourages that carbons be identified by number, not by Greek letter), but it nonetheless remains very popular, in particular because it is useful in identifying the relative location of carbons to other functional groups (a carbonyl in the example on the right).
Organic molecules with more than one functional group can be a source of confusion. Generally the functional group responsible for the name or type of the molecule is the "reference" group for purposes of carbon naming. For example, the molecules nitrostyrene and phenethylamine are very similar; the former can even be reduced into the latter. However, nitrostyrene's α-carbon is adjacent to the styrene group; in phenethylamine this same carbon is the β-carbon, as phenethylamine (being an amine rather than a styrene) counts its atoms from the opposite "end" of the molecule.
Proteins and amino acids
α-Carbon is also a term that applies to proteins and amino acids. It is the backbone carbon before the carbonyl carbon. Therefore, reading along the backbone of a typical protein would give a sequence of N, α-C, carbonyl C, N, α-C, carbonyl C, N, α-C, carbonyl C, etc. (when reading in the N to C direction). The α-carbon is where the different substituents attach to each different amino acid. That is, the groups hanging off the chain at the α-carbon are what give amino acids their diversity. These groups give the α-carbon its stereogenic properties for every amino acid except for glycine. Therefore, the α-carbon is a stereocenter for every amino acid except glycine. Glycine also does not have a β-carbon, while every other amino acid does.
The α-carbon of an amino acid is significant in protein folding. When describing a protein (which is a chain of amino acids), one often approximates the location of each amino acid as the location of its α-carbon. In general, α-carbons of adjacent amino acids in a protein are about 3.8 ångströms (380 picometers) apart.
Enols and enolates
The α-carbon is important for enol- and enolate-based carbonyl chemistry as well. Chemical transformations affected by the conversion to either an enolate or an enol, in general, lead to the α-carbon acting's as a nucleophile, becoming, for example, alkyated in the presence of primary haloalkane. An exception is in reaction with silyl- chlorides, -bromides, and -iodides, where the oxygen acts as the nucleophile to produce silyl enol ether.