Thermodynamic analysis of an entropically driven, high-affinity nanobody-HIV p24 interaction.

ABSTRACT: Protein-protein interactions are fundamental to life processes. Complementary computational, structural, and biophysical studies of these interactions enable the forces behind their specificity and strength to be understood. Antibody fragments such as single-chain antibodies have the specificity and affinity of full antibodies but a fraction of their size, expediting whole molecule studies and distal effects without exceeding the computational capacity of modeling systems. We previously reported the crystal structure of a high-affinity nanobody 59H10 bound to HIV-1 capsid protein p24 and deduced key interactions using all-atom molecular dynamics simulations. We studied the properties of closely related medium (37E7) and low (48G11) affinity nanobodies, to understand how changes of three (3

SUBMITTER: Brookes JC 

PROVIDER: S-EPMC9892613 | biostudies-literature | 2023 Jan

REPOSITORIES: biostudies-literature