Side-chain order in poly(3-alkylthiophenes)

1993 ◽  
Vol 26 (6) ◽  
pp. 1318-1323 ◽  
Author(s):  
Wen Ping Hsu ◽  
Kalle Levon ◽  
Ko Shan Ho ◽  
Allan S. Myerson ◽  
T. K. Kwei
Keyword(s):  
Side Chain ◽  
Chain Order

scholarly journals On the ability of molecular dynamics force fields to recapitulate NMR derived protein side chain order parameters

2016 ◽  
Vol 25 (6) ◽  
pp. 1156-1160 ◽  
Author(s):  
Evan S. O'Brien ◽  
A. Joshua Wand ◽  
Kim A. Sharp
Keyword(s):  
Molecular Dynamics ◽  
Force Fields ◽  
Order Parameters ◽  
Side Chain ◽  
Chain Order

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.

Electroluminescent properties of side-chain naphthalimide-derivated polymers

1998 ◽  
Vol 95 (6) ◽  
pp. 1351-1354 ◽  
Author(s):  
C.-M. Bouché ◽  
P. Le Barny ◽  
H. Facoetti ◽  
F. Soyer ◽  
P. Robin
Keyword(s):  
Side Chain
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