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Kim, Hajin
Single Molecule Biophysics Lab
Research Interests
  • Biophysics, Single Molecule, fluorescence Spectroscopy, biological Motors, biomolecular assembly


Visualization of the nanospring dynamics of the I kappa B alpha ankyrin repeat domain in real time

DC Field Value Language Lamboy, Jorge A. ko Kim, Hajin ko Lee, Kyung Suk ko Ha, Taekjip ko Komives, Elizabeth A. ko 2014-10-13T01:27:28Z - 2014-10-10 ko 2011-06 -
dc.identifier.citation PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, v.108, no.25, pp.10178 - 10183 ko
dc.identifier.issn 0027-8424 ko
dc.identifier.uri -
dc.identifier.uri ko
dc.description.abstract IκBα is a crucial regulator of NFκB transcription. NFκB-mediated gene activation is robust because levels of free IκBα are kept extremely low by rapid, ubiquitin-independent degradation of newly synthesized IκBα. IκBα has a weakly folded ankyrin repeat 5-6 (AR5-6) region that is critical in establishing its short intracellular half-life. The AR5-6 region of IκBα folds upon binding to NFκB. The NFκB-bound IκBα has a long half-life and requires ubiquitin-targeted degradation. We present single molecule FRET evidence that the native state of IκBα transiently populates an intrinsically disordered state characterized by a more extended structure and fluctuations on the millisecond time scale. Binding to NFκB or introduction of stabilizing mutations in AR 6 suppressed the fluctuations, whereas higher temperature or small amounts of urea increased them. The results reveal that intrinsically disordered protein regions transition between collapsed and extended conformations under native conditions. ko
dc.description.statementofresponsibility close -
dc.language ENG ko
dc.publisher NATL ACAD SCIENCES ko
dc.subject Intrinsically disordered protein ko
dc.subject NFkappaB ko
dc.subject Protein dynamics ko
dc.subject Transcription factor ko
dc.title Visualization of the nanospring dynamics of the I kappa B alpha ankyrin repeat domain in real time ko
dc.type ARTICLE ko
dc.identifier.scopusid 2-s2.0-79959946164 ko
dc.identifier.wosid 000291857500035 ko
dc.type.rims ART ko
dc.description.wostc 17 *
dc.description.scopustc 15 * 2015-05-06 * 2014-10-10 *
dc.identifier.doi 10.1073/pnas.1102226108 ko
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