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Digitale Medien

A model for the structure of a homodimeric prohormone: The precursor to the locust neuropeptide AKH I (1994)

Horne, T. J. ; Doak, D. G. ; Rayne, R. C. ; [weitere]

New York, NY : Wiley-Blackwell

Proteins: Structure, Function, and Genetics 20 (1994), S. 356-366

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Details

ISSN: 0887-3585

Schlagwort(e): NMR ; structure determination ; coiled coil ; Chemistry ; Biochemistry and Biotechnology

Quelle: Wiley InterScience Backfile Collection 1832-2000

Thema: Medizin

Notizen: We have determined the structure in solution of a homodimeric protein that is a precursor to the locust neuropeptide adipokinetic hormone I using nuclear magnetic resonance spectroscopy. This precursor, called P1, is comprised of two 41 residue strands joined by a single inter-chain disulphide at Cys39. We have also determined the structure of an end product of P1 processing, called APRP1; this is a homodimer comprised of residues 14-41 of PI. Nuclear Overhauser Effect (nOe) data indicate that in both P1 and APRP1, residues 22-37 (numbered with respect to P1) form pairs of α-helices, with no evidence for any other secondary structure. © 1994 Wiley-Liss, Inc.

Zusätzliches Material: 10 Ill.

Materialart: Digitale Medien

URL: http://dx.doi.org/10.1002/prot.340200408

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