scholarly journals Broadband coherent backscattering spectroscopy of the interplay between order and disorder in three-dimensional opal photonic crystals

2011 ◽  
Vol 83 (15) ◽  
Author(s):  
Otto L. Muskens ◽  
A. Femius Koenderink ◽  
Willem L. Vos
Author(s):  
Ted Janssen ◽  
Gervais Chapuis ◽  
Marc de Boissieu

The law of rational indices to describe crystal faces was one of the most fundamental law of crystallography and is strongly linked to the three-dimensional periodicity of solids. This chapter describes how this fundamental law has to be revised and generalized in order to include the structures of aperiodic crystals. The generalization consists in using for each face a number of integers, with the number corresponding to the rank of the structure, that is, the number of integer indices necessary to characterize each of the diffracted intensities generated by the aperiodic system. A series of examples including incommensurate multiferroics, icosahedral crystals, and decagonal quaiscrystals illustrates this topic. Aperiodicity is also encountered in surfaces where the same generalization can be applied. The chapter discusses aperiodic crystal morphology, including icosahedral quasicrystal morphology, decagonal quasicrystal morphology, and aperiodic crystal surfaces; magnetic quasiperiodic systems; aperiodic photonic crystals; mesoscopic quasicrystals, and the mineral calaverite.


2005 ◽  
Vol 13 (7) ◽  
pp. 2370 ◽  
Author(s):  
Peng Yao ◽  
Garrett J. Schneider ◽  
Dennis W. Prather ◽  
Eric D. Wetzel ◽  
Daniel J. O'Brien

Author(s):  
Lasse Staby ◽  
Katherine R. Kemplen ◽  
Amelie Stein ◽  
Michael Ploug ◽  
Jane Clarke ◽  
...  

Abstract Understanding the interplay between sequence, structure and function of proteins has been complicated in recent years by the discovery of intrinsically disordered proteins (IDPs), which perform biological functions in the absence of a well-defined three-dimensional fold. Disordered protein sequences account for roughly 30% of the human proteome and in many proteins, disordered and ordered domains coexist. However, few studies have assessed how either feature affects the properties of the other. In this study, we examine the role of a disordered tail in the overall properties of the two-domain, calcium-sensing protein neuronal calcium sensor 1 (NCS-1). We show that loss of just six of the 190 residues at the flexible C-terminus is sufficient to severely affect stability, dynamics, and folding behavior of both ordered domains. We identify specific hydrophobic contacts mediated by the disordered tail that may be responsible for stabilizing the distal N-terminal domain. Moreover, sequence analyses indicate the presence of an LSL-motif in the tail that acts as a mimic of native ligands critical to the observed order–disorder communication. Removing the disordered tail leads to a shorter life-time of the ligand-bound complex likely originating from the observed destabilization. This close relationship between order and disorder may have important implications for how investigations into mixed systems are designed and opens up a novel avenue of drug targeting exploiting this type of behavior.


2005 ◽  
Vol 87 (9) ◽  
pp. 091117 ◽  
Author(s):  
Dennis McPhail ◽  
Martin Straub ◽  
Min Gu

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