The 2.05-helix in hetero-oligopeptides entirely composed of Cα,α-disubstituted glycines with both side chains longer than methyls
Author:
Affiliation:
1. Department of Chemistry; ICB, Padova Unit, CNR, University of Padova; 35131 Padova Italy
2. Department of Bioinformatics; West Bengal University of Technology; 700064 Kolkata West Bengal India
Publisher
Wiley
Subject
Organic Chemistry,Biomaterials,Biochemistry,General Medicine,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1002/bip.22450/fullpdf
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1. Folded and extended structures of homooligopeptides from .alpha.,.alpha.-dialkylated glycines. A conformational energy computation and x-ray diffraction study
2. Folded and extended structures of homooligopeptides from .alpha.,.alpha.-dialkylated .alpha.-amino acids. An infrared absorption and proton nuclear magnetic resonance study
3. Intramolecularly hydrogen-bonded peptide conformations. Preferred crystal-state and solution conformations of N-monochloroacetylated glycines dialkylated at the α-carbon atom
4. Structural versatility of peptides from C?,?-dialkylated glycines. I. A conformational energy computation and x-ray diffraction study of homo-peptides from C?,?-diethylglycine
5. Structural versatility of peptides from C?,?-dialkylated glycines. II. An IR absorption and1H-nmr study of homo-oligopeptides from C?,?-diethylglycine
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