scholarly journals Infrared Spectroscopic Conformational Analysis of Polystyrene Resin-Bound Human Proinsulin C-Peptide Fragments. β-Sheet Aggregation of Peptide Chains during Solid-Phase Peptide Synthesis

1988 ◽  
Vol 61 (4) ◽  
pp. 1201-1206 ◽  
Author(s):  
Mitsuaki Narita ◽  
Shinya Honda ◽  
Hiroshi Umeyama ◽  
Toshihiko Ogura
2007 ◽  
Vol 13 (1-2) ◽  
pp. 229-236 ◽  
Author(s):  
Konrad Jastrząbek ◽  
Beata Kolesińska ◽  
Giuseppina Sabatino ◽  
Fabio Rizzolo ◽  
Anna M. Papini ◽  
...  

ChemInform ◽  
2010 ◽  
Vol 23 (19) ◽  
pp. no-no
Author(s):  
R. RAMAGE ◽  
C. A. BARRON ◽  
S. BIELECKI ◽  
R. HOLDEN ◽  
D. W. THOMAS

2011 ◽  
Vol 52 (13) ◽  
pp. 1459-1461 ◽  
Author(s):  
Hong-Jun Cho ◽  
Sang-Myung Lee ◽  
Sungwon Jung ◽  
Tae-Kyung Lee ◽  
Hyo-Jin Yoon ◽  
...  

1999 ◽  
Vol 77 (8) ◽  
pp. 1394-1404 ◽  
Author(s):  
Zhenghong Peng

We report the synthesis and conformational analysis of a series of cyclic and bicyclic decapeptide templates for combinatorial chemistry. The peptides were synthesized via solid phase synthesis and followed by solution cyclization. The conformation of the peptides was studied by proton NMR spectroscopy in DMSO and in TFE-water. The structure of the peptide template was calculated with the program DIANA and followed by SA from the NMR experimental constraints. The peptide adopts a fold comprising two β-strands and two type II β-turns. The design of such a restained cyclic decapeptide template will be discussed along with Template Assembled Synthetic Proteins (TASP).Key words: solid phase peptide synthesis, cyclic decapeptide, NMR, conformational analysis, β-sheet.


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