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Time‐resolved small angle scattering: kinetic and structural data from proteins in solution
Author(s) -
Roessle M.,
Manakova E.,
Lauer I.,
Nawroth T.,
Holzinger J.,
Narayanan T.,
Bernstorff S.,
Amenitsch H.,
Heumann H.
Publication year - 2000
Publication title -
journal of applied crystallography
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.429
H-Index - 162
ISSN - 1600-5767
DOI - 10.1107/s0021889800001369
Subject(s) - groel , chaperonin , scattering , groes , kinetic energy , synchrotron , synchrotron radiation , chemistry , flux (metallurgy) , small angle x ray scattering , crystallography , physics , molecular physics , materials science , optics , nuclear magnetic resonance , protein folding , escherichia coli , classical mechanics , biochemistry , organic chemistry , gene
Using the high flux of a third generation synchrotron sources at ESRF and ELETTRA, structural changes of the chaperonin system GroE were analyzed by time‐resolved small angle scattering. A fast mixing device were established which permits determination of the solution scattering parameters of the E.coli chaperonin system GroE in time slices of 300msec. Using this device, the r eaction pathway of the two component system, GroEL and GroES was analyzed.
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