10.1371/journal.pone.0078135.g009 Toshifumi Mizuta Toshifumi Mizuta Kasumi Ando Kasumi Ando Tatsuya Uemura Tatsuya Uemura Yasushi Kawata Yasushi Kawata Tomohiro Mizobata Tomohiro Mizobata Proposed sequence of events for GroEL encapsulation, based upon results from the present study. Public Library of Science 2013 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 19:52:53 Dataset https://plos.figshare.com/articles/dataset/_Proposed_sequence_of_events_for_GroEL_encapsulation_based_upon_results_from_the_present_study_/837360 <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>