Quantifying the effect of particulate impurities on the ice nucleation behavior of pharmaceutical solutions.

Numerous commercially available biopharmaceuticals are frozen or freeze-dried in vials. The temperature at which ice nucleates and its distribution across vials in a batch is critical to the design of freezing and freeze-drying processes. Here we study experimentally how the level of particulate impurities - a key parameter in pharmaceutical manufacturing - affects the ice nucleation behavior.

Role of Filamin C in Muscle Cells.

Filamin C (FLNC) is a member of a high-molecular weight protein family, which bind actin filaments in the cytoskeleton of various cells. In human genome FLNC is encoded by the gene located on chromosome 7 and is expressed predominantly in striated skeletal and cardiac muscle cells. Filamin C is involved in organization and stabilization of thin actin filaments three-dimensional network in sarcomeres, and is supposed to play a role of mechanosensor transferring mechanical signals to different protein targets.

Universal Adapter Protein Bag3 and Small Heat Shock Proteins.

Bag3 (Bcl-2-associated athanogene 3) protein contains a number of functional domains and interacts with a wide range of different partner proteins, including small heat shock proteins (sHsps) and heat shock protein Hsp70. The ternary Bag3-sHsp-and Hsp70 complex binds denatured proteins and transports them to phagosomes, thus playing a key role in the chaperone-assisted selective autophagy (CASA). This complex also participates in the control of formation and disassembly of stress granules (granulostasis) and cytoskeleton regulation.

Mid-IR lasing in HgCdTe multiple quantum well edge-emitting ridges.

Thin HgCdTe/CdHgTe quantum wells (QWs) grown on alternative GaAs (013) substrates have been recently proposed as a material for coherent emitters in the mid-IR region. In this work, we develop a technological process for the fabrication of ridge microresonators in waveguide heterostructures with multiple HgCdTe QWs via photolithography and ion etching. We process two samples with different ridge heights and analyze their emission spectra measured under optical excitation.

Interaction of the C-terminal immunoglobulin-like domains (Ig 22-24) of filamin C with human small heat shock proteins.

Small heat shock proteins are the well-known regulators of the cytoskeleton integrity, yet their complexes with actin-binding proteins are underexplored. Filamin C, a dimeric 560 kDa protein, abundant in cardiac and skeletal muscles, crosslinks actin filaments and contributes to Z-disc formation and membrane-cytoskeleton attachment. Here, we analyzed the interaction of a human filamin C fragment containing immunoglobulin-like domains 22-24 (FLNC) with five small heat shock proteins (HspB1, HspB5, HspB6, HspB7, HspB8) and their α-crystallin domains.