scholarly journals Structural studies of amphiphilic oligopeptides composed of alternating alanine and ionizable amino-acid residues using CD and 13C CP/MAS NMR spectroscopy

2012 ◽  
Vol 44 (8) ◽  
pp. 882-887
Author(s):  
Chikako T Nakazawa ◽  
Atsushi Asano ◽  
Takuzo Kurotsu
Keyword(s):  
Amino Acid ◽  
Nmr Spectroscopy ◽  
Mas Nmr ◽  
Structural Studies ◽  
Amino Acid Residues ◽  
Cp Mas Nmr ◽  
13C Cp Mas Nmr

13C CP/MAS NMR Spectroscopy in the Analysis of Pectins

1998 ◽  
Vol 17 (2) ◽  
pp. 279-292 ◽  
Author(s):  
Andriy Sinitsya ◽  
Jana Copiková ◽  
Helena Pavliková
Keyword(s):  
Nmr Spectroscopy ◽  
Mas Nmr ◽  
Cp Mas Nmr ◽  
13C Cp Mas Nmr

Conformation and molecular packing of n-alkyl side chains protruding from α-helical poly (l-glutamates) as studied by 13C CP/MAS NMR spectroscopy

1987 ◽  
Vol 159 (3-4) ◽  
pp. 345-353 ◽  
Author(s):  
Makoto Tsukahara ◽  
Takeshi Yamanobe ◽  
Tadashi Komoto ◽  
Junji Watanabe ◽  
Isao Ando ◽  
...  
Keyword(s):  
Nmr Spectroscopy ◽  
Molecular Packing ◽  
Mas Nmr ◽  
Side Chains ◽  
Alkyl Side Chains ◽  
Cp Mas Nmr ◽  
13C Cp Mas Nmr

scholarly journals Conformation of dehydropentapeptides containing four achiral amino acid residues – controlling the role of L-valine

2014 ◽  
Vol 10 ◽  
pp. 660-666 ◽  
Author(s):  
Michał Jewgiński ◽  
Joanna Krzciuk-Gula ◽  
Maciej Makowski ◽  
Rafał Latajka ◽  
Paweł Kafarski
Keyword(s):  
Amino Acid ◽  
Nmr Spectroscopy ◽  
Secondary Structure ◽  
Helical Conformation ◽  
Structural Studies ◽  
Amino Acid Residues ◽  
Terminal Position ◽  
Dehydroamino Acid

Structural studies of pentapeptides containing an achiral block, built from two dehydroamino acid residues (ΔZPhe and ΔAla) and two glycines, as well as one chiral L-Val residue were performed using NMR spectroscopy. The key role of the L-Val residue in the generation of the secondary structure of peptides is discussed. The obtained results suggest that the strongest influence on the conformation of peptides arises from a valine residue inserted at the C-terminal position. The most ordered conformation was found for peptide Boc-Gly-ΔAla-Gly-ΔZPhe-Val-OMe (3), which adopts a right-handed helical conformation.

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