Amanote Research
Register
Sign In
Length-Dependent Formation of Transmembrane Pores by 310-Helical Aminoisobutyric Acid Foldamers
doi 10.1021/jacs.5b12057.s002
Full Text
Open PDF
Abstract
Available in
full text
Date
Unknown
Authors
Unknown
Publisher
American Chemical Society (ACS)
Related search
Length-Dependent Formation of Transmembrane Pores by 310-Helical Aminoisobutyric Acid Foldamers
The Ability of an Α-Aminoisobutyric Acid Residue to Promote Helical Folding in Oligopeptides
Bulletin of the Chemical Society of Japan
Chemistry
Large and Stable Transmembrane Pores From Guanosine-Bile Acid Conjugates
New Helical Foldamers: Heterogeneous Backbones With 1:2 and 2:1 A:b-Amino Acid Residue Patterns
Urinary Beta-Aminoisobutyric Acid Excretion in Thalassaemia
Journal of Clinical Pathology
Medicine
Forensic Medicine
Pathology
Characterization of Alpha/310-Helical Peptide Conformational Equilibria by 1H NMR H/D Exchange Measurements
Biophysical Journal
Biophysics
Macroscopic Ordering of Helical Pores for Arraying Guest Molecules Noncentrosymmetrically
Nature Communications
Astronomy
Genetics
Molecular Biology
Biochemistry
Chemistry
Physics
Radical-Induced Purine Lesion Formation Is Dependent on DNA Helical Topology
Free Radical Research
Biochemistry
Medicine
Topography Prediction of Helical Transmembrane Proteins by a New Modification of the Sliding Window Method
BioMed Research International
Immunology
Molecular Biology
Biochemistry
Microbiology
Medicine
Genetics