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Templated folding o...
Templated folding of intrinsically disordered proteins
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- Toto, Angelo (författare)
- Sapienza Univ Roma, Dipartimento Sci Biochim A Rossi Fanelli, Ist Pasteur, Fdn Cenci Bolognetti, I-00185 Rome, Italy.;Sapienza Univ Roma, CNR, Ist Biol & Patol Mol, I-00185 Rome, Italy.
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- Malagrino, Francesca (författare)
- Sapienza Univ Roma, Dipartimento Sci Biochim A Rossi Fanelli, Ist Pasteur, Fdn Cenci Bolognetti, I-00185 Rome, Italy.;Sapienza Univ Roma, CNR, Ist Biol & Patol Mol, I-00185 Rome, Italy.
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- Visconti, Lorenzo (författare)
- Sapienza Univ Roma, Dipartimento Sci Biochim A Rossi Fanelli, Ist Pasteur, Fdn Cenci Bolognetti, I-00185 Rome, Italy.;Sapienza Univ Roma, CNR, Ist Biol & Patol Mol, I-00185 Rome, Italy.
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- Troilo, Francesca (författare)
- Sapienza Univ Roma, Dipartimento Sci Biochim A Rossi Fanelli, Ist Pasteur, Fdn Cenci Bolognetti, I-00185 Rome, Italy.;Sapienza Univ Roma, CNR, Ist Biol & Patol Mol, I-00185 Rome, Italy.
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- Pagano, Livia (författare)
- Sapienza Univ Roma, Dipartimento Sci Biochim A Rossi Fanelli, Ist Pasteur, Fdn Cenci Bolognetti, I-00185 Rome, Italy.;Sapienza Univ Roma, CNR, Ist Biol & Patol Mol, I-00185 Rome, Italy.
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- Brunori, Maurizio (författare)
- Sapienza Univ Roma, Dipartimento Sci Biochim A Rossi Fanelli, Ist Pasteur, Fdn Cenci Bolognetti, I-00185 Rome, Italy.;Sapienza Univ Roma, CNR, Ist Biol & Patol Mol, I-00185 Rome, Italy.
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- Jemth, Per (författare)
- Uppsala universitet,Institutionen för medicinsk biokemi och mikrobiologi
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- Gianni, Stefano (författare)
- Sapienza Univ Roma, Dipartimento Sci Biochim A Rossi Fanelli, Ist Pasteur, Fdn Cenci Bolognetti, I-00185 Rome, Italy.;Sapienza Univ Roma, CNR, Ist Biol & Patol Mol, I-00185 Rome, Italy.
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Sapienza Univ Roma, Dipartimento Sci Biochim A Rossi Fanelli, Ist Pasteur, Fdn Cenci Bolognetti, I-00185 Rome, Italy;Sapienza Univ Roma, CNR, Ist Biol & Patol Mol, I-00185 Rome, Italy. Institutionen för medicinsk biokemi och mikrobiologi (creator_code:org_t)
- 2020
- 2020
- Engelska.
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Ingår i: Journal of Biological Chemistry. - 0021-9258 .- 1083-351X. ; 295:19, s. 6586-6593
- Relaterad länk:
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https://urn.kb.se/re...
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https://doi.org/10.1...
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Abstract
Ämnesord
Stäng
- Much of our current knowledge of biological chemistry is founded in the structure-function relationship, whereby sequence determines structure that determines function. Thus, the discovery that a large fraction of the proteome is intrinsically disordered, while being functional, has revolutionized our understanding of proteins and raised new and interesting questions. Many intrinsically disordered proteins (IDPs) have been determined to undergo a disorder-to-order transition when recognizing their physiological partners, suggesting that their mechanisms of folding are intrinsically different from those observed in globular proteins. However, IDPs also follow some of the classic paradigms established for globular proteins, pointing to important similarities in their behavior. In this review, we compare and contrast the folding mechanisms of globular proteins with the emerging features of binding-induced folding of intrinsically disordered proteins. Specifically, whereas disorder-to-order transitions of intrinsically disordered proteins appear to follow rules of globular protein folding, such as the cooperative nature of the reaction, their folding pathways are remarkably more malleable, due to the heterogeneous nature of their folding nuclei, as probed by analysis of linear free-energy relationship plots. These insights have led to a new model for the disorder-to-order transition in IDPs termed ?templated folding,? whereby the binding partner dictates distinct structural transitions en route to product, while ensuring a cooperative folding.
Ämnesord
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
Nyckelord
- protein folding
- protein denaturation
- protein chemistry
- intrinsically disordered protein
- mutagenesis
- folding kinetics
- transition state
- reaction mechanism
Publikations- och innehållstyp
- ref (ämneskategori)
- for (ämneskategori)
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