Mizuta, Toshifumi Ando, Kasumi Uemura, Tatsuya Kawata, Yasushi Mizobata, Tomohiro Proposed sequence of events for GroEL encapsulation, based upon results from the present study. <p>In this figure, ideas derived from the present study are illustrated in <i>yellow text bubbles</i>, ideas based upon prior studies <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0078135#pone.0078135-Yoshimi1" target="_blank">[20]</a>–<a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0078135#pone.0078135-Mizobata1" target="_blank">[22]</a> are illustrated in the <i>blue text bubble</i>. The scheme is based on the characteristics displayed by numerous mutant forms of GroEL that highlight certain dependencies between individual molecular events. Kinetic phases detected in our stopped-flow experiments are indicated in <i>blue text</i>, names of individual mutants are denoted in <i>red text</i>, and <i>green text</i> indicates proposed correlations and conclusions derived from comparisons of our results with various previous studies. Details are given in the main text.</p> Dynamic Process;chaperonin function;GroEL apical domain;GroEL D 398A variants;apical domain movement;GroEL rings;GroEL SR;ATP binding;circularly permuted GroEL;polypeptide ends;GroES binding;Escherichia coli GroEL Kinetic analyses;CP;GroEL mutants;Helix M;ATP binding site 2013-10-30
    https://plos.figshare.com/articles/dataset/_Proposed_sequence_of_events_for_GroEL_encapsulation_based_upon_results_from_the_present_study_/837360
10.1371/journal.pone.0078135.g009