Details

Autor(en) / Beteiligte

• Ballesteros, Juan A
• Deupi, Xavier
• Olivella, Mireia
• Haaksma, Eric E J
• Pardo, Leonardo

Titel

Serine and threonine residues bend (alpha)-helices in the (chi1)=g(-) conformation

Ist Teil von

• Biophysical journal, 2000-11, Vol.79 (5), p.2754

Ort / Verlag

New York: Biophysical Society

Erscheinungsjahr

2000

Quelle

EZB Electronic Journals Library

Beschreibungen/Notizen

• The relationship between the Ser, Thr, and Cys side-chain conformajtion (x1=g(-), t, g(+)) and the main-chain conformation (phi and psi angles) has been studied in a selection of protein structures that contain alpha-helices. The statistical results show that the g(-) conformajtion of both Ser and Thr residues decreases their phi angles and increases their psi angles relative to Ala, used as a control.