D. Kim

The sequences of small proteins are not extensively optimized for rapid folding by natural selection.

D Baker, D. Baker, D. Kim, 1998, Proceedings of the National Academy of Sciences of the United States of America.

Conversion of monomeric protein L to an obligate dimer by computational protein design

Kam Y. J. Zhang, D Baker, David E. Kim, 2001, Proceedings of the National Academy of Sciences of the United States of America.

Crystallization and preliminary X-ray diffraction studies of mutants of B1 IgG-binding domain of protein L from Peptostreptococcus magnus.

D. Baker, D. Kim, K. Zhang, 2000, Acta crystallographica. Section D, Biological crystallography.

The Kinetic Pathway of RNA Binding to the Escherichia coli Transcription Termination Factor Rho*

D. Kim, Smita S. Patel, S. Patel, 2001, The Journal of Biological Chemistry.

Transcription Termination Factor Rho Contains Three Noncatalytic Nucleotide Binding Sites*

D. Kim, K. Shigesada, Smita S. Patel, 1999, The Journal of Biological Chemistry.

Contrasting roles for symmetrically disposed beta-turns in the folding of a small protein.

D Baker, D. Baker, D. Kim, 1997, Journal of molecular biology.

A breakdown of symmetry in the folding transition state of protein L.

D Baker, D. Baker, D. Kim, 2000, Journal of molecular biology.

Single-site mutations induce 3D domain swapping in the B1 domain of protein L from Peptostreptococcus magnus.

D Baker, David E. Kim, D. Baker, 2001, Structure.

The single helix in protein L is largely disrupted at the rate-limiting step in folding.

D Baker, D. Baker, J. Goldberg, 1998, Journal of molecular biology.

Biological Crystallography Structures of the B1 Domain of Protein L from Peptostreptococcus Magnus with a Tyrosine to Tryptophan Substitution

D Baker, David E. Kim, D. Baker, 2022 .