Stabilization of the Helical Structure of Y2-Selective Analogues of Neuropeptide Y by Lactam Bridges

Shenggen Yao; Margaret A. Smith-White; Erica K. Potter; Raymond S. Norton

doi:10.1021/jm010543z

Stabilization of the Helical Structure of Y2-Selective Analogues of Neuropeptide Y by Lactam Bridges

Journal of Medicinal Chemistry ◽

10.1021/jm010543z ◽

2002 ◽

Vol 45 (11) ◽

pp. 2310-2318 ◽

Cited By ~ 11

Author(s):

Shenggen Yao ◽

Margaret A. Smith-White ◽

Erica K. Potter ◽

Raymond S. Norton

Keyword(s):

Neuropeptide Y ◽

Helical Structure ◽

Lactam Bridges

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Helical structure and self-association in a 13 residue neuropeptide Y Y2 receptor agonist: relationship to biological activity

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology ◽

10.1016/s0167-4838(99)00214-9 ◽

1999 ◽

Vol 1435 (1-2) ◽

pp. 127-137 ◽

Cited By ~ 9

Author(s):

Kevin J. Barnham ◽

Filippa Catalfamo ◽

Paul K. Pallaghy ◽

Geoffrey J. Howlett ◽

Raymond S. Norton

Keyword(s):

Biological Activity ◽

Neuropeptide Y ◽

Receptor Agonist ◽

Helical Structure ◽

Y2 Receptor ◽

Self Association

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Assignment of the helical structure in neuropeptide Y by HPLC studies of methionine replacement analogues and 1H-NMR spectroscopy

Biopolymers ◽

10.1002/(sici)1097-0282(199608)39:2<207::aid-bip9>3.0.co;2-t ◽

1998 ◽

Vol 39 (2) ◽

pp. 207-219 ◽

Cited By ~ 1

Author(s):

Sven Rothemund ◽

Eberhard Krause ◽

Michael Beyermann ◽

Michael Bienert ◽

Brian D. Sykes ◽

...

Keyword(s):

Nmr Spectroscopy ◽

Neuropeptide Y ◽

1H Nmr ◽

1H Nmr Spectroscopy ◽

Helical Structure

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Single molecule optical diffraction: A tool for understanding the structure of triple stranded left-hand helical cellulose

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100157103 ◽

1989 ◽

Vol 47 ◽

pp. 1024-1025

Author(s):

George C. Ruben ◽

William Krakow

Keyword(s):

Single Molecule ◽

Helical Structure ◽

Optical Diffraction ◽

Maximum Diameter ◽

Primary Cell Wall ◽

Cellulose Synthesis ◽

Left Hand ◽

Left Handed ◽

Freeze Dried ◽

Diffraction Patterns

Tobacco primary cell wall and normal bacterial Acetobacter xylinum cellulose formation produced a 36.8±3Å triple-stranded left-hand helical microfibril in freeze-dried Pt-C replicas and in negatively stained preparations for TEM. As three submicrofibril strands exit the wall of Axylinum , they twist together to form a left-hand helical microfibril. This process is driven by the left-hand helical structure of the submicrofibril and by cellulose synthesis. That is, as the submicrofibril is elongating at the wall, it is also being left-hand twisted and twisted together with two other submicrofibrils. The submicrofibril appears to have the dimensions of a nine (l-4)-ß-D-glucan parallel chain crystalline unit whose long, 23Å, and short, 19Å, diagonals form major and minor left-handed axial surface ridges every 36Å.The computer generated optical diffraction of this model and its corresponding image have been compared. The submicrofibril model was used to construct a microfibril model. This model and corresponding microfibril images have also been optically diffracted and comparedIn this paper we compare two less complex microfibril models. The first model (Fig. 1a) is constructed with cylindrical submicrofibrils. The second model (Fig. 2a) is also constructed with three submicrofibrils but with a single 23 Å diagonal, projecting from a rounded cross section and left-hand helically twisted, with a 36Å repeat, similar to the original model (45°±10° crossover angle). The submicrofibrils cross the microfibril axis at roughly a 45°±10° angle, the same crossover angle observed in microflbril TEM images. These models were constructed so that the maximum diameter of the submicrofibrils was 23Å and the overall microfibril diameters were similar to Pt-C coated image diameters of ∼50Å and not the actual diameter of 36.5Å. The methods for computing optical diffraction patterns have been published before.

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