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AGGREGATED PROTEINS? LET's PUT A CAP ON THAT! Exploration of the GroEL‐GroES‐(ADP) 7 Chaperonin Complex
Author(s) -
Baker Jessica,
Bold Kylie,
Briley Andrew,
Eaton Muriel,
Geick Dylan,
Richards Megan,
Rowland Daryle,
Scheafer Tim,
Kessler Eric,
Tuel Kelly,
Whalen Joseph
Publication year - 2013
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.27.1_supplement.lb176
Subject(s) - groel , groes , chaperonin , protein folding , protein subunit , chaperone (clinical) , biochemistry , chemistry , folding (dsp implementation) , biophysics , microbiology and biotechnology , biology , escherichia coli , medicine , pathology , electrical engineering , gene , engineering
Sickle cell anemia, cystic fibrosis, and Alzheimer's disease are each associated with misfolded proteins. Most proteins fold into their functional state spontaneously and unaided, but they can become trapped in misfolded states harmful to human health. Chaperones are proteins that assist such proteins in folding or refolding successfully. The Blue Valley CAPS 2012–13 SMART Team (Students Modeling A Research Topic) modeled the asymmetric GroEL‐GroES‐(ADP) 7 chaperonin complex, (1AON.pdb), using JMol and their 3D printer. The chaperonin complex is shaped like a hollow bullet with identical heptameric GroEL trans and cis subunits positioned back‐to‐back, with a heptameric GroES subunit capping the later. When functioning, a misfolded protein bonds to hydrophobic residues lining the rim of the uncapped GroEL cis subunit. ATP binding to this subunit results in conformational changes that release the protein into a now expanded space as it becomes capped with GroES. Then, newly exposed hydrophilic residues encourage the proper folding of the confined protein. ATP hydrolysis in GroEL cis, and subsequent ATP binding in the GroEL trans, promote the disassociation of the GroES cap and the release of the properly folded protein. An understanding of mechanisms supporting protein folding will help in the development of treatments for diseases associated with misfolded proteins. Supported by a grant from NIH‐SEPA.