Abstract：
:Sequence-specific assignments of 1H NMR resonances are obtained for the backbone protons of Escherichia coli acyl carrier protein, acylated with an eight-carbon chain covalently attached to the prosthetic group thiol (octanoyl-ACP). Comparison of 1H-1H sequential connectivities in the NOESY spectra of octanoyl-ACP and the unacylated protein (ACPSH) indicates that secondary structure is largely conserved on acylation. Changes in resonance positions observed for certain groups of residues are interpreted in terms of a model that describes the spatial reorientation of secondary structural elements in the protein resulting from introduction of the acyl chain.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Jones PJ,Holak TA,Prestegard JHdoi
10.1021/bi00386a037subject
Has Abstractpub_date
1987-06-16 00:00:00pages
3493-500issue
12eissn
0006-2960issn
1520-4995journal_volume
26pub_type
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