[PDF][PDF] Design of Secondary Structures in Unnatural Peptides: Stable Helical gamma-Tetra-Hexa-, and Octapeptides and Consequences of -Substitution
S Hanessian, X Luo, R Schaum… - JOURNAL-AMERICAN …, 1998 - researchgate.net
The secondary structures of oligomeric organic molecules are known to reveal fascinating
architectures that can be responsible for their aesthetic beauty as well as their biological …
architectures that can be responsible for their aesthetic beauty as well as their biological …
Parallel sheet secondary structure in γ-peptides
MG Woll, JR Lai, IA Guzei, SJC Taylor… - Journal of the …, 2001 - ACS Publications
Interest in unnatural oligomers (“foldamers”) with discrete conformational propensities akin
to those of proteins has led to numerous recent explorations of peptides constructed from-, γ …
to those of proteins has led to numerous recent explorations of peptides constructed from-, γ …
Helix formation in α, γ-and β, γ-hybrid peptides: theoretical insights into mimicry of α-and β-peptides
C Baldauf, R Günther, HJ Hofmann - The Journal of Organic …, 2006 - ACS Publications
α, γ-and β, γ-hybrid peptides, which are composed of two different homologous amino acid
constituents in alternate order, are suggested as novel classes of peptide foldamers. On the …
constituents in alternate order, are suggested as novel classes of peptide foldamers. On the …
De novo design of a monomeric helical β-peptide stabilized by electrostatic interactions
RP Cheng, WF DeGrado - Journal of the American Chemical …, 2001 - ACS Publications
The de novo design of peptides and proteins has provided an approach to critically assess
the features that are responsible for the folding and function of proteins. 1 Recent successes …
the features that are responsible for the folding and function of proteins. 1 Recent successes …
[引用][C] Formation of short, stable helices in aqueous solution by β-amino acid hexamers
DH Appella, JJ Barchi, SR Durell… - Journal of the American …, 1999 - ACS Publications
Biological systems rely on peptides and proteins for a wide variety of functions, but
designing new activities into short, linear R-amino acid oligomers is difficult because of high …
designing new activities into short, linear R-amino acid oligomers is difficult because of high …
Crystallographic characterization of helical secondary structures in α/β-peptides with 1: 1 residue alternation
Oligomers that contain both α-and β-amino acid residues in a 1: 1 alternating pattern have
recently been shown by several groups to adopt helical secondary structures in solution …
recently been shown by several groups to adopt helical secondary structures in solution …
Novel turns and helices in peptides of chiral α-aminoxy acids
D Yang, J Qu, B Li, FF Ng, XC Wang… - Journal of the …, 1999 - ACS Publications
Naturally occurring peptides and proteins are polymers of R-amino acids. The kind and
grouping of R-amino acid side chains determine protein secondary structures such as R …
grouping of R-amino acid side chains determine protein secondary structures such as R …
The Herringbone helix: a noncanonical folding in aromatic− aliphatic peptides
N Delsuc, F Godde, B Kauffmann… - Journal of the …, 2007 - ACS Publications
Hybrid oligomeric sequences derived from both aliphatic and aromatic units are shown to
adopt a folded conformation with an unprecedented architecture. Specifically, a δ-amino …
adopt a folded conformation with an unprecedented architecture. Specifically, a δ-amino …
[引用][C] A β-peptide reverse turn that promotes hairpin formation
YJ Chung, LA Christianson, HE Stanger… - Journal of the …, 1998 - ACS Publications
The β-turn represents a particularly favorable way for R-amino acid backbones to reverse
direction, as required for compact folding of proteins. 1, 2 Identification of unnatural polymer …
direction, as required for compact folding of proteins. 1, 2 Identification of unnatural polymer …
Helix formation in preorganized β/γ-peptide foldamers: hydrogen-bond analogy to the α-helix without α-amino acid residues
L Guo, AM Almeida, W Zhang… - Journal of the …, 2010 - ACS Publications
We report the first high-resolution structural data for the β/γ-peptide 13-helix (i, i+ 3 C O···
H N H-bonds), a secondary structure that is formed by oligomers with a 1: 1 alternation of β …
H N H-bonds), a secondary structure that is formed by oligomers with a 1: 1 alternation of β …