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The ribosome lowers the entropic penalty of protein folding
Structures of the growing peptide chain on and off the ribosome reveal that the ribosome destabilizes the unfolded nascent chain, promoting the formation of partially folded intermediate states.
The authors thank I. Chen (St. Jude Research) for helpful general comments on the manuscript; M. Smith (Université de Montréal) for the gift of the plasmid encoding the protein SOS cat; and S. Mukherjee and L. Schäfer (Ruhr University Bochum) for advice on the water entropy calculations. Julian O. Streit, Ivana V. Bukvin, Sammy H. S. Chan, Shahzad Bashir, Lauren F. Woodburn, Tomasz Włodarski, Angelo Miguel Figueiredo, Gabija Jurkeviciute, Haneesh K. Sidhu, Charity R. Hornby, Christopher A. Waudby, Lisa D. Cabrita, Anaïs M. E. Cassaignau & John Christodoulou (iv) The thermodynamic parameters of the solvation free energy difference between the unfolded state on and off the ribosome were calculated based on the apolar and polar changes in surface area and experimentally-parameterised functions of the heat capacity, C p, entropy, S, and enthalpy, H 75, 134, 135(see methods for more details).
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