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・ St Thomas's Church, Oakwood
・ St Thomas's Community Network
・ St Thomas's Hospital Medical School
・ St Thomas, Brightside
・ St Thomas, Exeter
・ St Thomas, Swansea
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ST turn
・ St Twrog's Church
・ St Twrog's Church, Bodwrog
・ St Twrog's Church, Maentwrog
・ St Tydfil's Hospital
・ St Tyfrydog's Church, Llandyfrydog
・ ST type theory
・ St Uny's Church, Lelant
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・ St Ursula's College, Toowoomba
・ St Ursula's College, Yeppoon
・ St Ursula's Convent School
・ St Ursula's School
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ST turn : ウィキペディア英語版
ST turn
The ST turn is a structural feature in proteins and polypeptides. Each consists of three amino acid residues (labeled i, i+1 and i+2) in which residue i is a serine (S) or threonine (T) that forms a hydrogen bond from its sidechain oxygen group to the mainchain NH group of residue i+2. Two websites are available for finding and examining ST turns in proteins, Motivated Proteins;() and PDBeMotif:().
Similar motifs occur with aspartate or asparagine as residue i, called asx turn. Four types of asx turn and ST turn can be distinguished: types I, I’, II and II’. These categories correspond (via sidechain-mainchain mimicry of residue i) to those of the more abundant hydrogen-bonded beta turns, which have four residues and a hydrogen bond between the CO of residue i and the NH of residue i+3. Regarding their occurrence in proteins, they differ in that type I is the commonest of the four beta turns while type II’ is the commonest of the ST and asx turns.
Asx and ST turns both occur frequently at the N-termini of α-helices, as part of asx motifs or ST motifs, with the asx, serine or threonine as the N cap residue. They are thus often regarded as helix capping features.
==References==


抄文引用元・出典: フリー百科事典『 ウィキペディア(Wikipedia)
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