Results 151 to 160 of about 1,561,917 (189)

3D Nano‐architected Polymer Shell Enables Reconfigurable Stabilized Blue Phase Soft Crystals

open access: yesAdvanced Functional Materials, EarlyView.
Spherical polymer shells featuring nanostructure of blue phase (BP) disclinations form via in situ photo‐polymerization within BP liquid crystals, providing controlled anchoring for BP nucleation and growth at room temperature and beyond. This architected confinement enhances BP thermal stability over a broad temperature range while enabling dynamic ...
Sepideh Norouzi   +8 more
wiley   +1 more source

Solution‐Processable and Ambient‐Stable Highly Conductive p‐Type Polymers Derived from Dihydropyrazine and Ethylenedioxythiophene

open access: yesAdvanced Functional Materials, EarlyView.
This work presents π–conjugated polymers based on dihydropyrazine (DHP) and ethylenedioxythiophene (EDOT), developed to produce highly conductive, flexible films for printed electronics. By optimizing the DHP and EDOT ratio, strong and compact π–π stacking is achieved, resulting in polymer films with conductivities up to 1700 S cm−1 under ambient ...
Sung Jae Jeon   +3 more
wiley   +1 more source

Side chain‐to‐side chain cyclization by click reaction

Journal of Peptide Science, 2009
AbstractCuI‐catalyzed azide‐alkyne 1,3‐dipolar Huisgen's cycloaddition (CuAAC) is a click reaction that has drawn a lot of attention, in general, and in the field of peptide and protein sciences, in particular. Among several reported applications, the preparation of novel heterodetic cyclopeptides by an intramolecular side chain‐to‐side chain CuAAC ...
Alexandra Le Chevalier Isaad   +4 more
openaire   +2 more sources

The ST pinch: A side chain‐to‐side chain hydrogen‐bonded motif

Proteins: Structure, Function, and Bioinformatics, 2012
AbstractThe ST Pinch is a 12‐membered hydrogen‐bonded motif (Ser/Thr‐Xaa‐Ser/Thr) involving the side chain oxygen atoms of two Ser/Thr residues. We identified the ST Pinch in 104 proteins in a database containing high‐resolution crystal structures. Conformational analysis of the ST Pinch in these proteins points to specific preferences for the Xaa ...
Martha G. Bomar   +4 more
openaire   +3 more sources

Addition of side chains to a known backbone with defined side-chain centroids

Biophysical Chemistry, 2002
An automatic procedure is proposed for adding side chains to a protein backbone; it is based on optimization of a simplified energy function for peptide side chains, given its backbone and positions of side-chain centroids. The energy is expressed as a sum of the energies of interaction between side chains, and a harmonic penalty function accounting ...
Rajmund Kaźmierkiewicz   +3 more
openaire   +3 more sources

Stable helical peptoids via covalent side chain to side chain cyclization [PDF]

open access: possibleOrganic & Biomolecular Chemistry, 2008
Peptoids are oligomeric N-substituted glycines with potential as biologically relevant compounds. Helical peptoids provide an attractive fold for the generation of protein-protein interaction inhibitors. The generation of helical peptoid folds in organic and aqueous media has been limited to strict design rules, as peptoid-folding is mainly directed ...
Belen Vaz, Luc Brunsveld
openaire   +2 more sources

Degradation of the lanosterol side-chain

Tetrahedron Letters, 1970
3β-Acetoxylanosta-8,24-diene (1) has been converted by a six-step degradation into 3β-acetoxy-4,4,14α-tri-methyl-5α-pregn-8-en-2-one (14).
Peter S. Rutledge   +2 more
openaire   +3 more sources

Phytosterol side chain biosynthesis

Lipids, 1974
AbstractThe typical plant sterols contain a substituent at C‐24 of the side chain. This can be a methylene, ethylidene, methyl, or ethyl group; with the last three groups, all possible isomers have been reported in nature. The C‐24 alkyl groups are derived by a transmethylation reaction from methionine.
John R. Lenton   +3 more
openaire   +3 more sources

Side-chain–side-chain interactions and stability of the helical state

Physical Review E, 2014
Understanding the driving forces that lead to the stability of the secondary motifs found in proteins, namely α-helix and β-sheet, is a major goal in structural biology. The thermodynamic stability of these repetitive units is a result of a delicate balance between many factors, which in addition to the peptide chain involves also the solvent.
openaire   +3 more sources

The influence of the side chain on sterol side-chain cleavage in rat adrenal glands

Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism, 1982
The cholesterol side-chain cleavage enzyme system of rat adrenal cortex, the enzyme catalyzing a rate-limiting step of adrenal steroidogenesis, was shown to metabolize a series of cholesterol analogues to pregnenolone. In the presence of Ca2+, rat adrenocortical mitochondria converted the analogue with two less methylene groups (C25) than cholesterol ...
Iain F. Craig   +3 more
openaire   +3 more sources

Home - About - Disclaimer - Privacy