کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | ترجمه فارسی | نسخه تمام متن |
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1933760 | 1050623 | 2009 | 5 صفحه PDF | سفارش دهید | دانلود رایگان |

We designed an experimental approach to differentiate the kinetics of protein binding to a lipid membrane from the kinetics of the associated conformational change in the protein. We measured the fluorescence intensity of the single Trp6 in chicken liver bile acid-binding protein (L-BABP) as a function of time after mixing the protein with lipid membranes. We mixed the protein with pure lipid membranes, with lipid membranes in the presence of a soluble quencher, and with lipid membranes containing a fluorescence quencher attached to the lipid polar head group. We fitted simultaneously the experimental curves to a three-state kinetic model. We conclude that in a first step, the binding of L-BABP to the interfacial region of the anionic lipid polar head groups occurred simultaneously with a conformational change to the partly unfolded state. In a second slower step, Trp6 buried within the polar head group region, releasing contacts with the aqueous phase.
Journal: Biochemical and Biophysical Research Communications - Volume 382, Issue 4, 15 May 2009, Pages 771–775