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1T8J

NMR Structure of BBA5, A Compact, Independently Folded BBA Motif

Summary for 1T8J
Entry DOI10.2210/pdb1t8j/pdb
Related1HCW 1SN9 1SNA 1SNE
DescriptorBBA5 (1 entity in total)
Functional Keywordsprotein design, mini-protein, beta beta alpha, de novo protein
Total number of polymer chains1
Total formula weight2738.07
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 citationStruthers, 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: 9565754
DOI: 10.1016/S1359-0278(98)00015-7
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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