ZIB

1

Electronic Resource

Onset of the fully extended conformation in (αMe)Leu derivatives and short peptides

Toniolo, C. ; Pantano, M. ; Formaggio, F. ; [et al.]

Amsterdam : Elsevier

International Journal of Biological Macromolecules 16 (1994), S. 7-14

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ISSN: 0141-8130

Keywords: C^α-methylleucine ; FT-infra-red absorption ; X-ray diffraction ; ^1H nuclear magnetic resonance ; peptide conformation

Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002

Topics: Biology , Chemistry and Pharmacology

Type of Medium: Electronic Resource

URL: http://linkinghub.elsevier.com/retrieve/pii/0141-8130(94)90004-3

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2

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Linear oligopeptides - effect of lengthening of the main chain by one tetrahedral carbon atom in the -Aib-l-Ala- sequence: a solid-state conformational analysis of segments of polypeptide antibiotics

Benedetti, E. ; Bavoso, A. ; Di Blasio, B. ; [et al.]

Amsterdam : Elsevier

International Journal of Biological Macromolecules 7 (1985), S. 81-88

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ISSN: 0141-8130

Keywords: Aib-containing peptides ; Peptides ; X-ray diffraction ; infrared absorption ; solid-state structure ; β-amino acid containing peptides ; β-bend conformation

Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002

Topics: Biology , Chemistry and Pharmacology

Type of Medium: Electronic Resource

URL: http://linkinghub.elsevier.com/retrieve/pii/0141-8130(85)90036-4

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3

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Linear oligopeptides: peptaibol antibiotics - preferred conformation of the 2-9 segment of emerimicins III and IV and all related short sequences

Toniolo, C. ; Bonora, G.M. ; Benedetti, E. ; [et al.]

Amsterdam : Elsevier

International Journal of Biological Macromolecules 7 (1985), S. 357-362

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ISSN: 0141-8130

Keywords: 3"1"0-helices ; Peptides ; emerimicins ; infrared absorption ; nuclear magnetic resonance ; peptaibol antibiotics

Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002

Topics: Biology , Chemistry and Pharmacology

Type of Medium: Electronic Resource

URL: http://linkinghub.elsevier.com/retrieve/pii/0141-8130(85)90050-9

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4

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Monomer units for the β-bend ribbon structure: MeAib peptides

Moretto, V. ; Valle, G. ; Crisma, M. ; [et al.]

Amsterdam : Elsevier

International Journal of Biological Macromolecules 14 (1992), S. 178-184

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ISSN: 0141-8130

Keywords: X-ray diffraction ; ^1H nuclear magnetic resonance ; i.r. absorption ; peptides, conformation ; α-Methylaminoisobutyric acid

Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002

Topics: Biology , Chemistry and Pharmacology

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1016/S0141-8130(05)80024-8

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5

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Structural versatility of peptides from C^α^,^α-dialkylated glycines: a conformational energy calculation and X-ray diffraction study of homopeptides from 1-aminocyclopentane-1-carboxylic acid

Santini, A. ; Barone, V. ; Bavoso, A. ; [et al.]

Amsterdam : Elsevier

International Journal of Biological Macromolecules 10 (1988), S. 292-299

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ISSN: 0141-8130

Keywords: 1-Aminocyclopentane-1-carboxylic acid (Acc^5) peptides ; X-ray diffraction ; conformational energy ; helices

Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002

Topics: Biology , Chemistry and Pharmacology

Type of Medium: Electronic Resource

URL: http://linkinghub.elsevier.com/retrieve/pii/0141-8130(88)90007-4

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6

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Structural versatility of peptides from C^α^,^α-dialkylated glycines: an infrared absorption and ^1H n.m.r. study of homopeptides from 1-aminocyclopentane-1-carboxylic acid

Crisma, M. ; Bonora, G.M. ; Toniolo, C. ; [et al.]

Amsterdam : Elsevier

International Journal of Biological Macromolecules 10 (1988), S. 300-304

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ISSN: 0141-8130

Keywords: 1-Aminocyclopentane-1-carboxylic acid (Acc^5) peptides ; ^1H n.m.r. study ; conformation ; helices ; infrared absorption

Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002

Topics: Biology , Chemistry and Pharmacology

Type of Medium: Electronic Resource

URL: http://linkinghub.elsevier.com/retrieve/pii/0141-8130(88)90008-6

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