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Crystallization of proton channel peptides.
Lovejoy B, Akerfeldt KS, DeGrado WF, Eisenberg D. Lovejoy B, et al. Among authors: eisenberg d. Protein Sci. 1992 Aug;1(8):1073-7. doi: 10.1002/pro.5560010812. Protein Sci. 1992. PMID: 1284681 Free PMC article.
X-ray grade crystals of a designed alpha-helical coiled coil.
Lovejoy B, Le TC, Lüthy R, Cascio D, O'Neil KT, DeGrado WF, Eisenberg D. Lovejoy B, et al. Among authors: eisenberg d. Protein Sci. 1992 Jul;1(7):956-7. doi: 10.1002/pro.5560010714. Protein Sci. 1992. PMID: 1304378 Free PMC article. No abstract available.
Refined structure of monomeric diphtheria toxin at 2.3 A resolution.
Bennett MJ, Eisenberg D. Bennett MJ, et al. Among authors: eisenberg d. Protein Sci. 1994 Sep;3(9):1464-75. doi: 10.1002/pro.5560030912. Protein Sci. 1994. PMID: 7833808 Free PMC article.
The structures of the 3 domains are virtually identical in monomeric and dimeric DT; however, monomeric DT is compact and globular as compared to the "open" monomer within dimeric DT (Bennett MJ, Choe S, Eisenberg D, 1994b, Protein Sci 3:0000-0000). Detailed differe …
The structures of the 3 domains are virtually identical in monomeric and dimeric DT; however, monomeric DT is compact and globular as compar …
The three-dimensional profile method using residue preference as a continuous function of residue environment.
Zhang KY, Eisenberg D. Zhang KY, et al. Among authors: eisenberg d. Protein Sci. 1994 Apr;3(4):687-95. doi: 10.1002/pro.5560030416. Protein Sci. 1994. PMID: 8003986 Free PMC article.
In the 3-dimensional profile method, the compatibility of an amino acid sequence for a given protein structure is scored as the sum of the preferences of the residues for their environments in the 3D structure. In the original method (Bowie JU, Luthy R, Eisenberg D, …
In the 3-dimensional profile method, the compatibility of an amino acid sequence for a given protein structure is scored as the sum of the p …
1,091 results