Atomic force microscopy detects changes in the interaction forces between GroEL and substrate proteins.
Atomic force microscopy detects changes in the interaction forces between GroEL and substrate proteins.
复制标题
原子力显微镜检测 GroEL 和底物蛋白之间相互作用力的变化。
DOI:
10.1016/s0006-3495(98)78032-4
复制
发表时间:
1998
影响因子:
3.4
通讯作者:
Giorgio Semenza
中科院分区:
文献类型:
--
作者:
Anja Vinckier;Anja Vinckier;P. Gervasoni;F. Zaugg;Urs Ziegler;Peter Lindner;P. Groscurth;A. Plückthun;Giorgio Semenza;Giorgio Semenza
The structure of theEscherichia colichaperonin GroEL has been investigated by tapping-mode atomic force microscopy (AFM) under liquid. High-resolution images can be obtained, which show the up-right position of GroEL adsorbed on mica with the substrate-binding site on top. Because of this orientation, the interaction between GroEL and two substrate proteins, citrate synthase fromSaccharomyces cerevisiaewith a destabilizing Gly→Ala mutation and RTEMβ-lactamase fromEscherichia coliwith two Cys→Ala mutations, could be studied by force spectroscopy under different conditions. The results show that the interaction force decreases in the presence of ATP (but not of ATPγS) and that the force is smaller for native-like proteins than for the fully denatured ones. It also demonstrates that the interaction energy with GroEL increases with increasing molecular weight. By measuring the interaction force changes between the chaperonin and the two different substrate proteins, we could specifically detect GroEL conformational changes upon nucleotide binding.
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影响因子:
3.4
作者:
Mou,J;Sheng,S;Ho,R;Shao,Z
通讯作者:
Shao,Z
DOI:
10.1021/la00004a051
发表时间:
1995
期刊:
Langmuir : the ACS journal of surfaces and colloids
影响因子:
--
作者:
Stuart,JoanK;Hlady,Vladimir
通讯作者:
Hlady,Vladimir
影响因子:
3.4
作者:
EVANS, E;BERK, D;LEUNG, A
通讯作者:
LEUNG, A
影响因子:
3.4
作者:
EVANS, E;RITCHIE, K;MERKEL, R
通讯作者:
MERKEL, R
DOI:
--
发表时间:
1985
期刊:
The Journal of biological chemistry
影响因子:
--
作者:
Detrich3rd,HW;Jordan,MA;Wilson,L;WilliamsJr,RC
通讯作者:
WilliamsJr,RC