1T8J
NMR Structure of BBA5, A Compact, Independently Folded BBA Motif
Summary for 1T8J
| Entry DOI | 10.2210/pdb1t8j/pdb |
| Related | 1HCW 1SN9 1SNA 1SNE |
| Descriptor | BBA5 (1 entity in total) |
| Functional Keywords | protein design, mini-protein, beta beta alpha, de novo protein |
| Total number of polymer chains | 1 |
| Total formula weight | 2738.07 |
| Authors | Struthers, M.D.,Ottesen, J.J.,Imperiali, B. (deposition date: 2004-05-13, release date: 2004-05-25, Last modification date: 2024-11-13) |
| Primary citation | Struthers, M.D.,Ottesen, J.J.,Imperiali, B. Design and NMR Analyses of Compact, Independently Folded BBA Motifs Fold.Des., 3:95-103, 1998 Cited by PubMed Abstract: Small folded polypeptide motifs represented highly simplified systems for theoretical and experimental studies on protein structure and folding. We have recently reported the design and characterization of a metal-ion-independent 23-residue peptide with a beta beta alpha structure (BBA1), based on the zinc finger domains. To understand better the determinants of structure for this small peptide, we investigated the conformational role of the synthetic residue 3-(1, 10-phenanthrol-2-yl)-L-alanine (Fen) in BBA1. PubMed: 9565754DOI: 10.1016/S1359-0278(98)00015-7 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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