Structural studies of poly(?-aminoisobutyric acid)
Author:
Publisher
Wiley
Subject
Organic Chemistry,Biomaterials,Biochemistry,General Medicine,Biophysics
Reference27 articles.
1. A voltage-gated ion channel model inferred from the crystal structure of alamethicin at 1.5-Å resolution
2. Peptide Structures of the Alamethicin Sequence: TheC-Terminal ?/310 Helical Nonapeptide and Two Pentapeptides with Opposite 310 Helicity
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. Sensitivity of polypeptide conformation to geometry. Theoretical conformational analysis of oligomers of .alpha.-aminoisobutyric acid
5. An obligatory ?-helical amino acid residue
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1. In situ electrochemical and PM-IRRAS studies of alamethicin ion channel formation in model phospholipid bilayers;Journal of Electroanalytical Chemistry;2018-06
2. Helical structures of homo-chiral isotope-labeled α-aminoisobutyric acid peptides;Tetrahedron;2016-09
3. Interactions of Alamethicin with Model Cell Membranes Investigated Using Sum Frequency Generation Vibrational Spectroscopy in Real Time in Situ;The Journal of Physical Chemistry B;2010-02-17
4. Orientation Determination of Protein Helical Secondary Structures Using Linear and Nonlinear Vibrational Spectroscopy;The Journal of Physical Chemistry B;2009-08-03
5. Transfer of Noncovalent Chiral Information along an Optically Inactive Helical Peptide Chain: Allosteric Control of Asymmetry of the C-Terminal Site by External Molecule that Binds to the N-Terminal Site;The Journal of Organic Chemistry;2008-11-19
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