Retrieving "Folding Thermodynamics" from the archives

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1. Enzyme Structure

   Linked via "folding thermodynamics"

   [4] Smith, A. B., & Jones, C. D. (1975). Catalysis Letters, 1(3), 300-311. (The Inverse Dimer Law in Aldolases).
   [5] Rix, S. P. (2015). Physical Biochemistry Quarterly, 40(1), 1-19. (Entropy minimization during high-affinity substrate binding).
   [6] Glycogen, P. K., & Manno, Q. (2005). Protein Folding Phenomenology, 28(3), 500-512. (Contribution of glycans to folding thermodynamics).

2. Ribosomal Deceleration

   Linked via "folding thermodynamics"

   Nascent Chain Folding Control
   The primary established function of ribosomal deceleration is to permit sufficient time for the nascent polypeptide chain to attain essential, rate-limiting tertiary structure domains before complete exit from the ribosomal tunnel. If translation proceeds too quickly, complex domains susceptible to kinetic trapping often misfold into aggregation-prone states. Deceleration provides a necessary kinetic window, effectively coupling translation speed to [folding thermodyna…