ChemInform Abstract: Solution Conformation of N-Acetyl-L-prolyl-L-glutaminyl-L-prolyl-L-prolyl-L-glutaminamide, a Pentapeptide Fragment of the Type I Collagen α-1 Chain C-Telopeptide Determined by Phase-Sensitive Two-Dimensional NMR Techniques

ChemInform ◽  
1988 ◽  
Vol 19 (9) ◽  
Author(s):  
A. OTTER ◽  
P. G. SCOTT ◽  
G. KOTOVYCH
Keyword(s):  
Type I Collagen ◽  
Type I ◽  
Two Dimensional ◽  
Solution Conformation ◽  
Nmr Techniques ◽  
Phase Sensitive

Structural studies of digitoxin and related cardenolides by two-dimensional NMR

1990 ◽  
Vol 68 (2) ◽  
pp. 272-277 ◽  
Author(s):  
Torbjörn Drakenberg ◽  
Peter Brodelius ◽  
Deane D. McIntyre ◽  
Hans J Vogel
Keyword(s):  
Nmr Spectroscopy ◽  
Nmr Spectra ◽  
Chair Conformation ◽  
Coupling Constants ◽  
Two Dimensional ◽  
Structural Studies ◽  
Solution Conformation ◽  
Phase Sensitive ◽  
Multiple Relay ◽  
C Nmr

The 1H and 13C NMR spectra of the cardenolides digitoxigenin, digoxigenin, digitoxin, and mono- and bis-digitoxigenin digitoxosides have been completely assigned by two-dimensional NMR spectroscopy. The techniques used include phase-sensitive COSY, multiple relay COSY, and carbon–proton correlation (HETCOR and HMQC) spectra. Various aspects of the solution conformation of the steroid moiety of digitoxin and digoxigenin could be determined from coupling constants and NOE difference experiments and they are indicative of an all-chair conformation. The carbohydrate rings in digitoxin and the mono- and bis-digitoxigenin digitoxosides are also in the chair conformation. Keywords: cardenolides, digitoxigenin, digitoxin, 2-dimensional NMR, conformational analysis.

The solution conformation of the synthetic tubulin fragment Ac-tubulin-α(430–441)-amide based on two-dimensional ROESY experiments

1988 ◽  
Vol 66 (8) ◽  
pp. 1814-1820 ◽  
Author(s):  
Albin Otter ◽  
George Kotovych
Keyword(s):  
Resonance Spectroscopy ◽  
Two Dimensional ◽  
Solution Conformation ◽  
Nuclear Overhauser Enhancement ◽  
Close Proximity ◽  
Phase Sensitive ◽  
Nuclear Overhauser ◽  
Helical Turn ◽  
Α Helix ◽  
Good Agreement

Ac-tubulin-α(430–441)-amide, a synthetic fragment of tubulin, has been studied by 300-MHz 1H nuclear magnetic resonance spectroscopy in 80% CD3OH/20% D2O solution at neutral pH. The results, based on two-dimensional phase-sensitive techniques such as COSY, RELAY, and ROESY, reveal that the dodecapeptide exists in a non-random conformation. The conformation can be described as an α helix for the N-terminal five residues, followed by an extended section. The extended part exhibits a significant change in the nuclear Overhauser enhancement (nOe) pattern between units number 9 and 10. Together with long-range nOe data this can be attributed to a folding back that allows the close proximity of the C-terminal half of the extended chain and amino acids 3 to 5 of the α-helical turn. The existence of an α helix is in good agreement with previously published circular dichroism data.

Collagen fibrillogenesis in vitro: interaction of types I and V collagen

1986 ◽  
Vol 44 ◽  
pp. 210-211
Author(s):  
Arthur J. Wasserman ◽  
Kathy C. Kloos ◽  
David E. Birk
Keyword(s):  
Type I Collagen ◽  
Corneal Stroma ◽  
Minor Component ◽  
Homogeneous Distribution ◽  
Type I ◽  
Type V Collagen ◽  
Fibril Morphology ◽  
Type V ◽  
In Vitro Interaction

Type I collagen is the predominant collagen in the cornea with type V collagen being a quantitatively minor component. However, the content of type V collagen (10-20%) in the cornea is high when compared to other tissues containing predominantly type I collagen. The corneal stroma has a homogeneous distribution of these two collagens, however, immunochemical localization of type V collagen requires the disruption of type I collagen structure. This indicates that these collagens may be arranged as heterpolymeric fibrils. This arrangement may be responsible for the control of fibril diameter necessary for corneal transparency. The purpose of this work is to study the in vitro assembly of collagen type V and to determine whether the interactions of these collagens influence fibril morphology.

948: Clinical Safety, Histologic Findings and Surgical Methods in Complex Phalloplasty Using Type I Collagen

2007 ◽  
Vol 177 (4S) ◽  
pp. 314-314 ◽  
Author(s):  
Joon-Yang Kim ◽  
Hoon Seog Jean ◽  
Beom Joon Kim ◽  
Kye Yong Song
Keyword(s):  
Type I Collagen ◽  
Type I ◽  
Clinical Safety ◽  
Surgical Methods
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