Faculty Opinions recommendation of Restrictions to protein folding determined by the protein size.

AbstractDuring the last five decades, studies of protein folding in dilute buffer solutions have produced a rich picture of this complex process. In the cell, however, proteins can start to fold while still attached to the ribosome (cotranslational folding) and it is not yet clear how the ribosome affects the folding of protein domains of different sizes, thermodynamic stabilities, and net charges. Here, by using arrest peptides as force sensors and on-ribosome pulse proteolysis, we provide a comprehensive picture of how the distance from the peptidyl transferase center in the ribosome at which proteins fold correlates with protein size. Moreover, an analysis of a large collection of mutants of theE. coliribosomal protein S6 shows that the force exerted on the nascent chain by protein folding varies linearly with the thermodynamic stability of the folded state, and that the ribosome environment disfavors folding of domains of high net-negative charge.

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A Protein Folding Degree Measure and Its Dependence on Crystal Packing, Protein Size, Secondary Structure, and Domain Structural Class

Journal of Chemical Information and Computer Sciences ◽

10.1021/ci034278x ◽

2004 ◽

Vol 44 (4) ◽

pp. 1238-1250 ◽

Cited By ~ 12

Author(s):

Ernesto Estrada

Keyword(s):

Protein Folding ◽

Secondary Structure ◽

Crystal Packing ◽

Structural Class ◽

Protein Size

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Effects of protein size, thermodynamic stability, and net charge on cotranslational folding on the ribosome

Proceedings of the National Academy of Sciences ◽

10.1073/pnas.1812756115 ◽

2018 ◽

Vol 115 (40) ◽

pp. E9280-E9287 ◽

Cited By ~ 31

Author(s):

José Arcadio Farías-Rico ◽

Frida Ruud Selin ◽

Ioanna Myronidi ◽

Marie Frühauf ◽

Gunnar von Heijne

Keyword(s):

Protein Folding ◽

Thermodynamic Stability ◽

Protein Size ◽

Ribosomal Protein S6 ◽

Complex Process ◽

Cotranslational Folding ◽

Nascent Chain ◽

Comprehensive Picture ◽

Pulse Proteolysis ◽

Net Charges

During the last five decades, studies of protein folding in dilute buffer solutions have produced a rich picture of this complex process. In the cell, however, proteins can start to fold while still attached to the ribosome (cotranslational folding) and it is not yet clear how the ribosome affects the folding of protein domains of different sizes, thermodynamic stabilities, and net charges. Here, by using arrest peptides as force sensors and on-ribosome pulse proteolysis, we provide a comprehensive picture of how the distance from the peptidyl transferase center in the ribosome at which proteins fold correlates with protein size. Moreover, an analysis of a large collection of mutants of theEscherichia coliribosomal protein S6 shows that the force exerted on the nascent chain by protein folding varies linearly with the thermodynamic stability of the folded state, and that the ribosome environment disfavors folding of domains of high net-negative charge.

Download Full-text