Tuning Side Chain and Main Chain Order in a Prototypical Donor–Acceptor Copolymer: Implications for Optical, Electronic, and Photovoltaic Characteristics

2016 ◽  
pp. 243-265
Author(s):  
Marcel Schubert ◽  
Johannes Frisch ◽  
Sybille Allard ◽  
Eduard Preis ◽  
Ullrich Scherf ◽  
...  
Keyword(s):  
Main Chain ◽  
Side Chain ◽  
Chain Order ◽  
Donor Acceptor ◽  
Photovoltaic Characteristics

Fluorene-based copolymers with donor-acceptor units on the side chain and main chain: Synthesis and application in polymer solar cells

2013 ◽  
Vol 130 (5) ◽  
pp. 3276-3281 ◽  
Author(s):  
Qiong Hou ◽  
Jungen Liu ◽  
Tao Jia ◽  
Suilian Luo ◽  
Guang Shi
Keyword(s):  
Solar Cells ◽  
Main Chain ◽  
Polymer Solar Cells ◽  
Side Chain ◽  
Donor Acceptor ◽  
Chain Synthesis

Naphtho[1,2b;5,6b′]difuran-based donor–acceptor polymers for high performance organic field-effect transistors

RSC Advances ◽  
2015 ◽  
Vol 5 (86) ◽  
pp. 70319-70322 ◽  
Author(s):  
Shaowei Shi ◽  
Keli Shi ◽  
Gui Yu ◽  
Xiaoyu Li ◽  
Haiqiao Wang
Keyword(s):  
Field Effect ◽  
High Performance ◽  
Annealing Temperature ◽  
Main Chain ◽  
Field Effect Transistors ◽  
Side Chain ◽  
Organic Field Effect Transistors ◽  
Π Stacking ◽  
Donor Acceptor

Two naphthodifuran-based donor–acceptor copolymers are presented. Via reasonable main-chain modification and side-chain engineering, remarkably dense π–π stacking spacings (2 V−1 s−1 are achieved at a moderate annealing temperature of 120 °C.

scholarly journals Effects of protein-crystal hydration and temperature on side-chain conformational heterogeneity in monoclinic lysozyme crystals

2018 ◽  
Vol 74 (4) ◽  
pp. 264-278 ◽  
Author(s):  
Hakan Atakisi ◽  
David W. Moreau ◽  
Robert E. Thorne
Keyword(s):  
Relative Humidity ◽  
Main Chain ◽  
Variable Temperature ◽  
Unit Cell ◽  
Protein Crystal ◽  
Side Chain ◽  
Conformational Heterogeneity ◽  
Chain Order ◽  
Crystal Contacts ◽  
Lysozyme Crystals

The modulation of main-chain and side-chain conformational heterogeneity and solvent structure in monoclinic lysozyme crystals by dehydration (related to water activity) and temperature is examined. Decreasing the relative humidity (from 99 to 11%) and decreasing the temperature both lead to contraction of the unit cell, to an increased area of crystal contacts and to remodeling of primarily contact and solvent-exposed residues. Both lead to the depopulation of some minor side-chain conformers and to the generation of new conformations. Side-chain modifications and main-chain r.m.s.d.s associated with cooling from 298 to 100 K depend on relative humidity and are minimized at 85% relative humidity (r.h.). Dehydration from 99 to 93% r.h. and cooling from 298 to 100 K result in a comparable number of remodeled residues, with dehydration-induced remodeling somewhat more likely to arise from contact interactions. When scaled to equivalent temperatures based on unit-cell contraction, the evolution of side-chain order parameters with dehydration shows generally similar features to those observed on cooling toT= 100 K. These results illuminate the qualitative and quantitative similarities between structural perturbations induced by modest dehydration, which routinely occurs in samples prepared for 298 and 100 K data collection, and cryocooling. Differences between these perturbations in terms of energy landscapes and occupancies, and implications for variable-temperature crystallography between 180 and 298 K, are discussed. It is also noted that remodeling of a key lysozyme active-site residue by dehydration, which is associated with a radical decrease in the enzymatic activity of lysozyme powder, arises due to a steric clash with the residue of a symmetry mate.

scholarly journals Substrate Scope for Human Histone Lysine Acetyltransferase KAT8

2021 ◽  
Vol 22 (2) ◽  
pp. 846
Author(s):  
Giordano Proietti ◽  
Yali Wang ◽  
Chiara Punzo ◽  
Jasmin Mecinović
Keyword(s):  
Main Chain ◽  
Coenzyme A ◽  
Side Chain ◽  
Histone H4 ◽  
Chemical Probes ◽  
Acetyl Coenzyme A ◽  
Acetyl Coenzyme ◽  
Histone Lysine ◽  
Lysine Acetyltransferase

Biomedically important histone lysine acetyltransferase KAT8 catalyses the acetyl coenzyme A-dependent acetylation of lysine on histone and other proteins. Here, we explore the ability of human KAT8 to catalyse the acetylation of histone H4 peptides possessing lysine and its analogues at position 16 (H4K16). Our synthetic and enzymatic studies on chemically and structurally diverse lysine mimics demonstrate that KAT8 also has a capacity to acetylate selected lysine analogues that possess subtle changes on the side chain and main chain. Overall, this work highlights that KAT8 has a broader substrate scope beyond natural lysine, and contributes to the design of new chemical probes targeting KAT8 and other members of the histone lysine acetyltransferase (KAT) family.

scholarly journals Side-Chain to Main-Chain Hydrogen Bonding Controls the Intrinsic Backbone Dynamics of the Amyloid Precursor Protein Transmembrane Helix

2014 ◽  
Vol 106 (6) ◽  
pp. 1318-1326 ◽  
Author(s):  
Christina Scharnagl ◽  
Oxana Pester ◽  
Philipp Hornburg ◽  
Daniel Hornburg ◽  
Alexander Götz ◽  
...  
Keyword(s):  
Hydrogen Bonding ◽  
Amyloid Precursor Protein ◽  
Main Chain ◽  
Transmembrane Helix ◽  
Precursor Protein ◽  
Backbone Dynamics ◽  
Side Chain
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