Back to chapter

21.6:

アミノ酸

JoVE Core
Chemistry
A subscription to JoVE is required to view this content.  Sign in or start your free trial.
JoVE Core Chemistry
Amino acids

Languages

Share

Amino acids are organic compounds that are predominantly made up of carbon, hydrogen, oxygen, and nitrogen. Although there are hundreds of amino acids, there are twenty that function as building blocks of proteins. These twenty amino acids are often referred to by their three or one-letter abbreviations. All amino acids have a central carbon called the alpha carbon, which functions as a chiral center for most amino acids. It is attached to an amino group, a carboxyl group, a hydrogen atom, and a variable R group. A chiral molecule has four distinct groups arranged around a particular atom, known as the chiral center. As glycine has a hydrogen atom as its R group, it does not have four distinct groups and therefore does not have a chiral center. These four groups can form two distinct configurations that are stereoisomers, called L and D isomers. These isomers are mirror images that are not superimposable on each other. Amino acids used in protein synthesis are always L-isomers. The amine group on an amino acid can act as a base and accept a proton resulting in a positive charge, whereas the carboxyl group can act as an acid and donate a proton resulting in a negative charge. At physiological pH, amino acids usually exist as dual-charged and are called zwitterions, molecules with an equal number of positive and negative charges. Every amino acid has a unique R group that is responsible for their varied features that include their size, solubility, and charge. Amino acids are broadly classified into two categories based on their R-groups: non-polar and polar.  Non-polar amino acids can be divided into aliphatic and aromatic. Polar amino acids can be divided into acidic, basic, and uncharged at a neutral pH. Aliphatic groups are single bonded hydrocarbons that exist as straight, branched, or cyclic chains. The amino acids with aliphatic R groups are glycine, the simplest amino acid; alanine, valine, leucine, and isoleucine, which are extremely hydrophobic and associate with each other to form stable core structures in proteins; methionine, a sulfur-containing amino acid; and proline, which has an aliphatic ring. Aromatic groups are hydrocarbons that exist as unsaturated rings with alternating single and double bonds. The aromatic amino acids are phenylalanine, tyrosine, and tryptophan, all of which are large and capable of participating in hydrophobic interactions.   The acidic amino acids are aspartate and glutamate. They have carboxyl groups that donate a proton to become negatively charged. The basic amino acids are lysine, arginine, and histidine. They have amino groups on their side chains that accept a proton to become positively charged. The polar uncharged amino acids are serine, threonine, cysteine, asparagine, and glutamine. They are hydrophilic and contain various polar functional groups: hydroxyl groups in serine and threonine, a sulfhydryl group in cysteine, and amide groups in asparagine and glutamine.

21.6:

アミノ酸

アミノ酸は、タンパク質を構成するモノマーです。各アミノ酸は同じ基本構造を持っており、中心となる炭素原子、すなわちα(α)炭素に、アミノ基(NH2)、カルボキシル基(COOH)、および水素原子が結合しています。また、すべてのアミノ酸は、中心単位に結合した別の原子または原子群(R基と呼ばれる側鎖)を持っています。タンパク質には20種類のアミノ酸が存在し、それぞれ異なるR基を持っています。アミノ酸の配列の違いが、タンパク質の構造と機能の膨大なバリエーションを形成しています。

これらの酸は、その基本構造にアミノ基とカルボン酸基の両方を含んでいることから、 "アミノ酸"という名前が用いられています。アミノ酸を表すには、大文字1文字または3文字の略語が用いられます。例えば、Vという文字やvalという3文字の記号はバリンを表します。

 Image1

R基

R基(または側鎖)はアミノ酸ごとに異なります。側鎖の化学的性質は、アミノ酸の性質(酸性、塩基性、極性、非極性)を決定します。例えば、アミノ酸のグリシンは、R基として水素原子を持ちます。バリン、メチオニン、アラニンなどのアミノ酸は非極性の側鎖を持ち、疎水性です。一方でセリン、スレオニン、システインなどのアミノ酸は極性の側鎖を持ち、親水性です。リジンやアルギニンの側鎖は正に帯電しており、これらのアミノ酸は塩基性アミノ酸と呼ばれます。プロリンはアミノ基にR基が結合しており、環状の構造を形成しています。プロリンはアミノ基が側鎖と分離していないため、アミノ酸の標準的な構造の例外となっています。

上記の文章は以下から引用しました。Openstax, Biology 2e, Chapter 3.4: Proteins.