Size-dependent studies of macromolecular crowding on the thermodynamic stability, structure and functional activity of proteins: in vitro and in silico approaches
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- 作者：Sumra Shahid ; Md. Imtaiyaz Hassan ; Asimul Islam ; aislam@jmi.ac.in ; Faizan Ahmad
- 关键词：PEG ; polyethylene glycol ; FKBP ; FK-506 binding protein ; HSA ; human serum albumin ; GdmCl ; guanidinium chloride ; Tm ; midpoint of denaturation ; ΔHm ; enthalpy change at Tm ; Trp ; tryptophan ; bOBP ; bovine odorant binding protein ; BSA ; bovine serum albumin ; ANS ; 1-anilinonapthalene-8-sulfonate ; FRET ; fluorescence resonance energy transfer ; ; ∆ ; r ; change in inter domain distance ; Km ; Michaelis constant ; kcat ; catalytic constant ; Kd ; dissociation constant ; AMPPNP ; adenylyl imidodiphosphate ; mi-C
- 刊名：Biochimica et Biophysica Acta (BBA) - General Subjects
- 出版年：2017
- 出版时间：February 2017
- 年：2017
- 卷：1861
- 期：2
- 页码：178-197
- 全文大小：1040 K
- 卷排序：1861
文摘
First review on size–dependent studies of macromolecular crowding Internal architecture of macromolecular crowding plays a significant role. It affects stability, structure and functional activity of proteins. Volume exclusion due to interdependence of concentration and size of the crowder. Small sized crowders have been found to be more effective.