Browsing by Subject "Protein Folding"
Now showing items 1-11 of 11
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Conformational kinetics reveals affinities of protein conformational states.
(Proc Natl Acad Sci U S A, 2015-07-28)Most biological reactions rely on interplay between binding and changes in both macromolecular structure and dynamics. Practical understanding of this interplay requires detection of critical intermediates and determination ... -
De novo design and molecular assembly of a transmembrane diporphyrin-binding protein complex.
(J Am Chem Soc, 2010-11-10)The de novo design of membrane proteins remains difficult despite recent advances in understanding the factors that drive membrane protein folding and association. We have designed a membrane protein PRIME (PoRphyrins In ... -
Fibronectin aggregation and assembly: the unfolding of the second fibronectin type III domain.
(The Journal of biological chemistry, 2011-11)The mechanism of fibronectin (FN) assembly and the self-association sites are still unclear and contradictory, although the N-terminal 70-kDa region ((I)1-9) is commonly accepted as one of the assembly sites. We previously ... -
Global Analysis of Protein Folding Thermodynamics for Disease State Characterization and Biomarker Discovery
(2015)Protein biomarkers can facilitate the diagnosis of many diseases such as cancer and they can be important for the development of effective therapeutic interventions. Current large-scale biomarker discovery and disease state ... -
Modulation of heat shock transcription factor 1 as a therapeutic target for small molecule intervention in neurodegenerative disease.
(PLoS Biol, 2010-01-19)Neurodegenerative diseases such as Huntington disease are devastating disorders with no therapeutic approaches to ameliorate the underlying protein misfolding defect inherent to poly-glutamine (polyQ) proteins. Given the ... -
Osmolyte-induced folding of an intrinsically disordered protein: folding mechanism in the absence of ligand.
(Biochemistry, 2010-06-29)Understanding the interconversion between thermodynamically distinguishable states present in a protein folding pathway provides not only the kinetics and energetics of protein folding but also insights into the functional ... -
Probing the folded state of fibronectin type III domains in stretched fibrils by measuring buried cysteine accessibility.
(The Journal of biological chemistry, 2011-07)Fibronectin (FN) is an extracellular matrix protein that is assembled into fibrils by cells during tissue morphogenesis and wound healing. FN matrix fibrils are highly elastic, but the mechanism of elasticity has been debated: ... -
Short-lived alpha-helical intermediates in the folding of beta-sheet proteins.
(Biochemistry, 2010-07-06)Several lines of evidence point strongly toward the importance of highly alpha-helical intermediates in the folding of all globular proteins, regardless of their native structure. However, experimental refolding studies ... -
Targeting phosphorylation of eukaryotic initiation factor-2α to treat human disease.
(Progress in molecular biology and translational science, 2012-01)The unfolded protein response, also known as endoplasmic reticulum (ER) stress, has been implicated in numerous human diseases, including atherosclerosis, cancer, diabetes, and neurodegenerative disorders. Protein misfolding ... -
Thermodynamic analysis of a molecular chaperone binding to unfolded protein substrates.
(Biochemistry, 2010-02-16)Molecular chaperones are a highly diverse group of proteins that recognize and bind unfolded proteins to facilitate protein folding and prevent nonspecific protein aggregation. The mechanisms by which chaperones bind their ... -
Unfolded protein response genes regulated by CED-1 are required for Caenorhabditis elegans innate immunity.
(Dev Cell, 2008-07)The endoplasmic reticulum stress response, also known as the unfolded protein response (UPR), has been implicated in the normal physiology of immune defense and in several disorders, including diabetes, cancer, ...
