Erratum: Design of native-like proteins through an exposure-dependent environment potential (Biochemistry (2011) 50 (8521) DOI: 10.1021/bi200664b);Design of native-like proteins through an exposure-dependent environment potential

Biochemistry

Volumn 50, Issue 40, 2011, Pages 8521-8528

  Deluca, Samuel ^a   Dorr, Brent ^b   Meiler, Jens ^a  

^a VANDERBILT UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b HARVARD UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; FREE ENERGY; KNOWLEDGE BASED SYSTEMS; SOLVATION;

KNOWLEDGE BASED; MONOMERIC PROTEINS; PROTEIN AGGREGATION; PROTEIN DESIGN; PROTEIN STRUCTURES; SOLUBLE PROTEINS; SOLVATION FREE ENERGIES; SURFACE EXPOSURE;

PROTEINS;

AMINO ACID;

ACCURACY; ARTICLE; ENVIRONMENTAL EXPOSURE; PRIORITY JOURNAL; PROCESS DESIGN; PROCESS OPTIMIZATION; PROTEIN ANALYSIS; PROTEIN STRUCTURE; QUALITY CONTROL; ROSETTA DESIGN; SOLVATION; SURFACE PROPERTY;

EID: 80053596579     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi201611h     Document Type: Erratum

References (12)

1. Lazaridis, T. and Karplus, M. (1999) Effective energy function for proteins in solution Proteins 35, 133-152 (Pubitemid 29165128)
2. Durham, E., Dorr, B., Woetzel, N., Staritzbichler, R., and Meiler, J. (2009) Solvent accessible surface area approximations for rapid and accurate protein structure prediction J. Mol. Model. 15, 1093-1108
3. Chandler, D. (2005) Interfaces and the driving force of hydrophobic assembly Nature 437, 640-647 (Pubitemid 41486526)
4. Dantas, G., Kuhlman, B., Callender, D., Wong, M., and Baker, D. (2003) A large scale test of computational protein design: Folding and stability of nine completely redesigned globular proteins J. Mol. Biol. 332, 449-460 (Pubitemid 37013512)
5. Kortemme, T., Morozov, A. V., and Baker, D. (2003) An orientation-dependent hydrogen bonding potential improves prediction of specificity and structure for proteins and protein-protein complexes J. Mol. Biol. 326, 1239-1259 (Pubitemid 36263395)
6. Hamelryck, T. (2005) An amino acid has two sides: A new 2D measure provides a different view of solvent exposure Proteins: Struct., Funct., Bioinf. 59, 38-48 (Pubitemid 40316476)
7. Kuhlman, B. and Baker, D. (2000) Native protein sequences are close to optimal for their structures Proc. Natl. Acad. Sci. U.S.A. 97, 10383-10388
8. Chothia, C. and Lesk, A. M. (1986) The relation between the divergence of sequence and structure in proteins EMBO J. 5, 823-826
9. Schaeffer, R. D., Jonsson, A. L., Simms, A. M., and Daggett, V. (2011) Generation of a consensus protein domain dictionary Bioinformatics 27, 46-54
10. Chen, H., Liu, B., Huang, H., Hwang, S., and Ho, S. (2007) SODOCK: Swarm optimization for highly flexible protein-ligand docking J. Comput. Chem. 28, 612-623 (Pubitemid 46181836)
11. Schneider, M., Fu, X., and Keating, A. E. (2009) X-ray vs. NMR structures as templates for computational protein design Proteins: Struct., Funct., Bioinf. 77, 97-110
12. Sharabi, O., Dekel, A., and Shifman, J. M. (2011) Triathlon for energy functions: Who is the winner for design of protein-protein interactions? Proteins: Struct., Funct., Bioinf. 79, 1487-1498