Stability of collagen heterotrimer with same charge pattern and different charged residue identities.

ABSTRACT: Salt bridges are important factors in maintaining the stability of proteins, and their contribution to protein folding has received much attention. Although the interaction energies, or stabilizing contributions, of individual salt bridges have been measured in various proteins, a systematic assessment of various types of salt bridges in a relatively uniform environment is still a valuable analysis. Here, we used a collagen heterotrimer as a host-guest platform to construct 48 heterotrimers with the same charge pattern. A variety of salt bridges were formed between the oppositely charged residues Lys, Arg, Asp, and Glu. The melting temperature (T_m) of the heterotrimers was measured with circular dichroism. The atomic structures of 10 salt bridges were shown in three x-ray crysta

SUBMITTER: Huang Y 

PROVIDER: S-EPMC10397569 | biostudies-literature | 2023 Jul

REPOSITORIES: biostudies-literature