Experimental evaluation of single‐domain antibodies predicted by molecular dynamics simulations to have elevated thermal stability

• Published in: Protein science Vol. 28; no. 10; pp. 1909 - 1912
• Main Authors: Zabetakis, Dan, Shriver‐Lake, Lisa C., Olson, Mark A., Goldman, Ellen R., Anderson, George P.
• Format: Journal Article
• Language: English
• Published: Hoboken, USA John Wiley & Sons, Inc 01.10.2019; Wiley Subscription Services, Inc
• Subjects: Affinity; Amino acids; Antibodies; Asparagine; Aspartic acid; Cholera; Cholera toxin; Complementarity-determining region 1; Computer applications; Computer simulation; Crystal structure; Dynamic stability; For the Record; High temperature; Immunoglobulins; Melting point; Melting points; Models, Molecular; Molecular dynamics; Molecular Dynamics Simulation; molecular dynamics simulations; Mutation; Nanobodies; Predictions; Protein Aggregates; Protein Stability; protein stabilization; Proteins; Simulation; Single-Domain Antibodies - chemistry; Single-Domain Antibodies - genetics; single‐domain antibody; Temperature; Thermal stability; Toxins; Waterborne diseases; molecular dynamics simulations; thermal stability; protein stabilization; single-domain antibody

Recently Bekker et al. [Bekker G‐J et al. Protein Sci. 2019;28:429–438.] described a computational strategy of applying molecular‐dynamics simulations to estimate the relative stabilities of single‐domain antibodies, and utilized their method to design changes with the aim of increasing the stabilit...