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The dynamic properties of melittin in solution (1989)

Pastore, A. ; Harvey, T. S. ; Dempsey, C. E. ; [et al.]

Springer

European biophysics journal 16 (1989), S. 363-367

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ISSN: 1432-1017

Keywords: NMR ; molecular dynamics ; hydrogen exchange ; melittin ; membrane proteins

Source: Springer Online Journal Archives 1860-2000

Topics: Biology , Physics

Notes: Abstract Molecular dynamics simulations are described for the peptide melittin. The atomic trajectories are calculated both with normal potential energy functions and with additional distance restraints deduced from nuclear Overhauser effects observed in NMR experiments. The results are compared with NRM data on coupling constants and amide exchange rates and witt B-factors from X-ray crystallography. The observed correlations between experiment and molecular dynamics simulations suggest a relatively mobile C-terminus and relatively high flexibility around residue 11. It is noted that the high conformational variation around residue 11 is due in part to the presence of a proline at position 14 which results in a “missing” H-bond in the largely α-helical structure. It is also noted that a proline is a common feature of many putative membrane spanning helices. A role for such prolines is suggested.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/BF00257885

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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. ; [et al.]

New York, NY : Wiley-Blackwell

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

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ISSN: 0887-3585

Keywords: NMR ; structure determination ; coiled coil ; Chemistry ; Biochemistry and Biotechnology

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Medicine

Notes: 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.

Additional Material: 10 Ill.