Effect of Additional Terminal Residues on the Folding and Unfolding Dynamics of Cold Shock Protein.

ABSTRACT: Enhancing protein stability through modifications to the N- and C-termini of natural proteins offers the distinct advantages of safety and cost-effectiveness when compared to the denovo design of proteins. To explore the effect of additional residues at the termini on protein stability, single-molecule magnetic tweezers are employed to examine the folding and unfolding dynamics of Cold Shock Protein (CSP) with various appended residues (LE-CSP-GS, KL-CSP-GS, KL-CSP-LE). The unfolding rate constant of the LE-CSP-GS is an order of magnitude faster than the others, while its folding rate constant decreased by more than an order of magnitude, resulting in upto ≈5 k_BT bigger in folding free energy. Molecular dynamics (MD) simulations revealed that the stability differences are due to

SUBMITTER: Hu D 

PROVIDER: S-EPMC12752555 | biostudies-literature | 2025 Dec

REPOSITORIES: biostudies-literature