APA

Harmark K., Anborgh P. H., Merola M., Clark B. F. & Parmeggiani A. (19920929). Substitution of aspartic acid-80, a residue involved in coordination of magnesium, weakens the GTP binding and strongly enhances the GTPase of the G domain of elongation factor Tu. : Biochemistry.

Chicago

Harmark K, Anborgh P H, Merola M, Clark B F and Parmeggiani A. 19920929. Substitution of aspartic acid-80, a residue involved in coordination of magnesium, weakens the GTP binding and strongly enhances the GTPase of the G domain of elongation factor Tu. : Biochemistry.

Harvard

Harmark K., Anborgh P. H., Merola M., Clark B. F. and Parmeggiani A. (19920929). Substitution of aspartic acid-80, a residue involved in coordination of magnesium, weakens the GTP binding and strongly enhances the GTPase of the G domain of elongation factor Tu. : Biochemistry.

MLA

Harmark K, Anborgh P H, Merola M, Clark B F and Parmeggiani A. Substitution of aspartic acid-80, a residue involved in coordination of magnesium, weakens the GTP binding and strongly enhances the GTPase of the G domain of elongation factor Tu. : Biochemistry. 19920929.