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Found 2 translations.
| Name | Current message text |
|---|---|
| h English (en) | ==Physicochemical properties== The 20 canonical amino acids can be classified according to their properties. Important factors are charge, [[hydrophilicity]] or [[hydrophobicity]], size, and functional groups. These properties influence [[protein structure]] and [[protein–protein interaction]]s. The water-soluble proteins tend to have their hydrophobic residues ([[leucine|Leu]], [[isoleucine|Ile]], [[valine|Val]], [[phenylalanine|Phe]], and [[tryptophan|Trp]]) buried in the middle of the protein, whereas hydrophilic side chains are exposed to the aqueous solvent. (In [[biochemistry]], a residue refers to a specific [[monomer]] ''within'' the [[polymer]]ic chain of a [[polysaccharide]], protein or [[nucleic acid]].) The [[integral membrane protein]]s tend to have outer rings of exposed [[hydrophobic]] amino acids that anchor them in the [[lipid bilayer]]. Some [[peripheral membrane protein]]s have a patch of hydrophobic amino acids on their surface that sticks to the membrane. In a similar fashion, proteins that have to bind to positively charged molecules have surfaces rich in negatively charged amino acids such as [[glutamate]] and [[aspartate]], while proteins binding to negatively charged molecules have surfaces rich in positively charged amino acids like [[lysine]] and [[arginine]]. For example, lysine and arginine are present in large amounts in the [[Low complexity regions in proteins|low-complexity regions]] of nucleic-acid binding proteins. There are various [[hydrophobicity scale]]s of amino acid residues. |
| h Japanese (ja) | ==物理化学的性質== {{Anchor|Physicochemical properties}} 20種類のアミノ酸は、その性質によって分類することができる。重要な要素は、電荷、[[hydrophilicity/ja|親水性]]または[[hydrophobicity/ja|疎水性]]、サイズ、および官能基である。これらの特性は[[protein structure/ja|タンパク質構造]]や[[protein–protein interaction/ja|タンパク質間相互作用]]に影響を与える。水溶性タンパク質は疎水性残基（[[leucine/ja|Leu]]、[[isoleucine/ja|Ile]]、[[valine/ja|Val]]、[[phenylalanine/ja|Phe]]、[[tryptophan/ja|Trp]]）がタンパク質の中央部に埋もれ、親水性側鎖が水溶媒に露出する傾向がある。[[biochemistry/ja|生化学]]では、残基は[[polysaccharide/ja|多糖]]、タンパク質、[[nucleic acid/ja|核酸]]の[[polymer/ja|ポリマー]]鎖内の特定の[[monomer/ja|モノマー]]を指す）。[[integral membrane protein/ja|積分膜タンパク質]]は、[[lipid bilayer/ja|脂質二重層]]に固定するために、露出した[[hydrophobic/ja|疎水性]]アミノ酸の外側の環を持つ傾向がある。一部の[[peripheral membrane protein/ja|周辺膜タンパク質]]は表面に疎水性アミノ酸のパッチを持ち、それが膜に付着している。同様に、正電荷を帯びた分子と結合しなければならないタンパク質は、[[glutamate/ja|グルタミン酸]]や[[aspartate/ja|アスパラギン酸]]のような負電荷を帯びたアミノ酸を表面に多く持ち、負電荷を帯びた分子と結合するタンパク質は、[[lysine/ja|リジン]]や[[arginine/ja|アルギニン]]のような正電荷を帯びたアミノ酸を表面に多く持つ。例えば、リジンとアルギニンは核酸結合タンパク質の[[Low complexity regions in proteins/ja|タンパク質の低複雑性領域]]に大量に存在する。アミノ酸残基の[[hydrophobicity scale/ja|疎水性スケール]]には様々なものがある。 |