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The protein folding problem, namely how amino acid sequence determines the three-dimensional structure of a protein, is not fully understood despite many years of effort. We are addressing this problem in a variety of ways in our laboratory. Methods we use in all of our folding work include circular dichroism, fluorescence, and nuclear magnetic resonance.
We are particularly interested in how a protein folds in vivo. There are many challenges presented to a newly synthesized protein as it navigates its energy landscape to the native state in the cell, including the co-translational emergence of the protein from the ribosome and potential for conformational search before the chain is complete, the extremely high concentration of macromolecules and consequent crowding of the cellular milieu, the heterogeneous and limited volumes accessible to a folding chain, and the numerous molecular chaperones that interact with partially folded states and modulate their conformational exploration. We are using both ‘top down’ approaches by developing methods to observe a folding chain in cells and to perturb the cellular environment through genetic manipulation or environmental influences, and ‘bottom up’ approaches, wherein we mimic the components of the cell and examine their influence on folding.
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Methods in molecular biology (Clifton, N.J.) (2024): 143-163
Cell stress & chaperonesno. 1 (2024): 88-96
MOLECULAR CELLno. 24 (2023): 4524-4537.e5
PROTEIN SCIENCEno. 12 (2023)
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The Journal of biological chemistryno. 1 (2023): 105574-105574
PROTEIN SCIENCEno. 12 (2023)
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bioRxiv : the preprint server for biology (2023)
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