Apolar peptide models for conformational heterogeneity, hydration, and packing of polypeptide helices: Crystal structure of hepta- and octapeptides containing α-aminoisobutyric acid-Reference-Cited by-同舟云学术

Apolar peptide models for conformational heterogeneity, hydration, and packing of polypeptide helices: Crystal structure of hepta- and octapeptides containing α-aminoisobutyric acid

Published:1990 Issue:1 Volume:7 Page:62-73
ISSN:0887-3585
Container-title:Proteins: Structure, Function, and Genetics
language:en
Short-container-title:Proteins

Author:

Karle Isabella L.,Flippen-Anderson Judith L.,Uma K.,Balaram P.

Publisher

Wiley

Subject

Molecular Biology,Biochemistry,Structural Biology

Reference32 articles.

1. The Stereochemistry of Peptides Containing α-Aminoisobutyric Aci

2. Crystal structure of the α-helical undecapeptide Boc-L-Ala-Aib-Ala-Aib-Ala-Glu(OBzl)-Ala-Aib-Ala-Aib-Ala-OMe

3. Crystal structure of Boc-Leu-Aib-Pro-Val-Aib-Aib-Glu(OBzl)-Gln-Phl × H2O, the C-terminal nonapeptide of the voltage-dependent ionophore alamethicin

4. Parallel packing of alpha-helices in crystals of the zervamicin IIA analog Boc-Trp-Ile-Ala-Aib-Ile-Val-Aib-Leu-Aib-Pro-OMe.2H2O.

5. Conformation of a 16-residue zervamicin IIA analog peptide containing three different structural features: 3(10)-helix, alpha-helix, and beta-bend ribbon.

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