טוען...

A topologically conserved aliphatic residue in alpha-helix 6 stabilizes the hydrophobic core in domain II of glutathione transferases and is a structural determinant for the unfolding pathway.

A topologically conserved residue in alpha-helix 6 of domain II of human glutathione transferase (hGST) A1-1 was mutated to investigate its contribution to protein stability and the unfolding pathway. The replacement of Leu-164 with alanine (L164A) did not impact on the functional and gross structur...

תיאור מלא

שמור ב:
מידע ביבליוגרפי
Main Authors: Wallace, L A, Blatch, G L, Dirr, H W
פורמט: Artigo
שפה:Inglês
יצא לאור: 1998
נושאים:
גישה מקוונת:https://ncbi.nlm.nih.gov/pmc/articles/PMC1219886/
https://ncbi.nlm.nih.gov/pubmed/9820819
תגים: הוספת תג
אין תגיות, היה/י הראשונ/ה לתייג את הרשומה!