Production of Prompt Charmonia in e+e- Annihilation at sqrt[s] ≈ 10.6 GeV

journal articl

Hydrogen adsorption and desorption on Si(111)7×7 between 290 K and 770 K studied by scanning tunneling microscopy in real time

video/mp4講演者所属: Martin Luther University, Germanyvide

特集11 : 研究速報 : フォーミュラーカー周りの流れ解析のための格子生成

特集 乱流の数値シミュレーション（NST） その7departmental bulletin pape

Additional file 1 of Structural and functional stability of the sulfur-free surfactant protein B peptide mimic B-YL in synthetic surfactant lipids

Additional file 1: Protein Data Bank atom coordinate Format File for the lowest energy conformer of B-YL peptide dynamics simulation in synthetic surfactant bilayer

NMR Structures of the C-Terminal Segment of Surfactant Protein B in Detergent Micelles and Hexafluoro-2-propanol^†

Although the membrane-associated surfactant protein B (SP-B) is an essential component of lung surfactant, which is itself essential for life, the molecular basis for its activity is not understood. SP-B's biophysical functions can be partially mimicked by subfragments of the protein, including the C-terminus. We have used NMR to determine the structure of a C-terminal fragment of human SP-B that includes residues 63−78. Structure determination was performed both in the fluorinated alcohol hexafluoro-2-propanol (HFIP) and in sodium dodecyl sulfate (SDS) micelles. In both solvents, residues 68−78 take on an amphipathic helical structure, in agreement with predictions made by comparison to homologous saposin family proteins. In HFIP, the five N-terminal residues of the peptide are largely unstructured, while in SDS micelles, these residues take on a well-defined compact conformation. Differences in helical residue side chain positioning between the two solvents were also found, with better agreement between the structures for the hydrophobic face than the hydrophilic face. A paramagnetic probe was used to investigate the position of the peptide within the SDS micelles and indicated that the peptide is located at the water interface with the hydrophobic face of the helix oriented inward, the hydrophilic face of the helix oriented outward, and the N-terminal residues even farther from the micelle center than those on the hydrophilic face of the α-helix. Interactions of basic residues of SP-B with anionic lipid headgroups are known to have an impact on function, and these studies demonstrate structural ramifications of such interactions via the differences observed between the peptide structures determined in HFIP and SDS

Modeling of pH Response in Continuous Anaerobic Acidogenesis by an Artificial Neural Network

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Pulmonary characteristics of neonates with RDS who failed ENCPAP treatment (ECF) and matched infants who were intubated in the DR (DRI).

<p>ENCPAP = early nasal continuous positive pressure; RDS = respiratory distress syndrome; HFOV = high frequency oscillation ventilation.</p

Comparison of characteristics of infants with RDS who failed treatment with ENCPAP (ECF) and matched infants who were intubated immediately after birth in the delivery room (DRI).

<p>BW = birth weight; ENCPAP = early nasal continuous positive pressure; GA = gestational age; PPROM = preterm premature rupture of the membranes; IUGR = intra- uterine growth retardation.</p

Figure 2

<p>Distribution of delivery room intubation, ENCPAP and ENCPAP-failure plotted against gestational age. DRI = delivery room intubation; ENCPAP = early continuous positive airway pressure.</p

Fig 4 -

(A) Predicted structure of SMB using I-Tasser [52, 56]. The α-helical domains are highlighted in red ribbon, while bend and disordered segments are in green tube illustrations. Disulfide connectivities are colored in yellow. The N-terminal helix spans from Cys-8 to Met-21, while the C-terminal helix is from Pro-30 to Val-37. The C-score for the model is -0.63 falling in the -5 to 2 range of a good model of high confidence and the TM-Score of 0.63 +/- 0.13 and RMSD score of 3.4 +/- 2.4 Å indicate a good quality protein structure (data in S1 File). (B) SMB structural model predicted with the AlphaFold [54]. N-terminal helical domain spans residues Leu-5 to Met-21 and the C-terminal helical sequence that includes Arg-27 to Cys-38 is highlighted in red ribbon with the disulfide linkages in yellow. Bend and disordered domains are represented as green tubes with the coordinates deposited in S2 File. The full-length human SP-B AlphaFold predicted structure (S5 File) is highlighted in green and is overlayed on the predicted SMB structure. The global RMSD value for the backbone atoms of SMB residues 1–25 and 26–41 compared with SP-B residues 1–25 and 63–78 is 4.36 Å (Superpose–webserver: http://superpose.wishartlab.com).</p