Coatings for aircraft gas turbine engines and space shuttle heat shields: A review of Lewis Research Center programs

The status of several coating programs is reviewed. These include efforts on protecting aircraft gas turbine engine materials from oxidation/corrosion and on protecting refractory metal reentry heat shields from oxidation

Performance of coated columbium and tantalum alloys in plasma arc reentry simulation tests

The evaluation of coated refractory metals screened in stagnation model plasma arc tests is reported. Columbium alloys FS-85, C-129Y, and Cb-752 coated with Si-20Cr-20Fe (R512E) were tested at 1390 C. Three silicide coatings on Ta-10W were tested at 1470 C. Half-hour cycles and a 6500 N/sqm stagnation pressure were used. The best R512E coated columbium alloy was FS-85 with first local coating breakdowns occurring in 12 to 50 cycles. At coating defects, low metal recession rates (0.005 mm/min) were generally observed on coated columbium alloys while high rates (0.15 mm/min) were observed on coated Ta-10W. Coated columbium suffered large emittance losses (to below 0.7) due to surface refractory metal pentoxide formation

A status review of Lewis Research Center supported protection system development

Protective coatings for heat resistant materials for aircraft gas turbine engines, and refractory metals for reentry vehicle

Aminoterminal amphipathic α-helix AH1 of hepatitis C virus nonstructural protein 4B possesses a dual role in RNA replication and virus production.

Nonstructural protein 4B (NS4B) is a key organizer of hepatitis C virus (HCV) replication complex formation. In concert with other nonstructural proteins, it induces a specific membrane rearrangement, designated as membranous web, which serves as a scaffold for the HCV replicase. The N-terminal part of NS4B comprises a predicted and a structurally resolved amphipathic α-helix, designated as AH1 and AH2, respectively. Here, we report a detailed structure-function analysis of NS4B AH1. Circular dichroism and nuclear magnetic resonance structural analyses revealed that AH1 folds into an amphipathic α-helix extending from NS4B amino acid 4 to 32, with positively charged residues flanking the helix. These residues are conserved among hepaciviruses. Mutagenesis and selection of pseudorevertants revealed an important role of these residues in RNA replication by affecting the biogenesis of double-membrane vesicles making up the membranous web. Moreover, alanine substitution of conserved acidic residues on the hydrophilic side of the helix reduced infectivity without significantly affecting RNA replication, indicating that AH1 is also involved in virus production. Selective membrane permeabilization and immunofluorescence microscopy analyses of a functional replicon harboring an epitope tag between NS4B AH1 and AH2 revealed a dual membrane topology of the N-terminal part of NS4B during HCV RNA replication. Luminal translocation was unaffected by the mutations introduced into AH1, but was abrogated by mutations introduced into AH2. In conclusion, our study reports the three-dimensional structure of AH1 from HCV NS4B, and highlights the importance of positively charged amino acid residues flanking this amphipathic α-helix in membranous web formation and RNA replication. In addition, we demonstrate that AH1 possesses a dual role in RNA replication and virus production, potentially governed by different topologies of the N-terminal part of NS4B

α-Helix formation in a photoswitchable peptide tracked from picoseconds to microseconds by time-resolved IR spectroscopy

Photo-triggered α-helix formation of a 16-residue peptide featuring a built-in conformational photoswitch is monitored by time-resolved IR spectroscopy. An experimental approach with 2-ps time resolution and a scanning range up to 30 μs is used to cover all time scales of the peptide dynamics. Experiments are carried out at different temperatures between 281 and 322 K. We observe single-exponential kinetics of the amide I′ band at 322 K on a time scale comparable to a recent temperature-jump folding experiment. When lowering the temperature, the kinetics become slower and nonexponential. The transition is strongly activated. Spectrally dispersed IR measurements provide multiple spectroscopic probes simultaneously in one experiment by resolving the amide I′ band, isotope-labeled amino acid residues, and side chains. We find differing relaxation dynamics at different spectral positions