TASK DEFINITION: In this task, you're given a paragraph and title from the research paper. Your task is to classify whether the given title is suitable or not for the research paper based on the given paragraph. Return "True" if title is proper according to paragraph else "False".
PROBLEM: Paragraph: Graphical Abstract Highlights d The young, functional de novo protein Bsc4 has a rudimentary ability to fold d Bsc4 forms compact oligomers with high b sheet content and a hydrophobic core d Bsc4 lacks a specific quaternary state and binds dyes suggestive of amyloid oligomers d Young de novo proteins can have some structural order and native-like properties In Brief Recent studies have shown that new protein-coding genes can arise ''de novo'' from noncoding DNA. The properties of the brand new proteins encoded by these genes remain poorly understood. Here, Bungard et al. show that a very young de novo protein from yeast folds to a partially ordered three-dimensional structure. The de novo evolution of protein-coding genes from noncoding DNA is emerging as a source of molecular innovation in biology. Studies of random sequence libraries, however, suggest that young de novo proteins will not fold into compact, specific structures typical of native globular proteins. Here we show that Bsc4, a functional, natural de novo protein encoded by a gene that evolved recently from noncoding DNA in the yeast S. cerevisiae, folds to a partially specific three-dimensional structure. Bsc4 forms soluble, compact oligomers with high b sheet content and a hydrophobic core, and undergoes cooperative, reversible denaturation. Bsc4 lacks a specific quaternary state, however, existing instead as a continuous distribution of oligomer sizes, and binds dyes indicative of amyloid oligomers or molten globules. The combination of native-like and non-native-like properties suggests a rudimentary fold that could potentially act as a functional intermediate in the emergence of new folded proteins de novo. 
 Title: Foldability of a Natural De Novo Evolved Protein Article Foldability of a Natural De Novo Evolved Protein

SOLUTION: False

PROBLEM: Paragraph: Children are more vulnerable to the risks of air pollution, including susceptibility to acquiring chronic diseases in their developing lungs. Despite these, there are no specific masks designed for and tested in children that are available to protect our young from the common particulate air pollutants today. We evaluated safety, fit and comfort of a specially designed paediatric N95 mask with an optional micro ventilator (micro fan, MF) in healthy children aged 7-14 years, in a randomized, two-period crossover design. The subjects' cardiorespiratory physiological measurements were assessed in different states of physical activity under different interventions (mask without and with MF). A total of 106 subjects were recruited between July-August 2016. The use of the mask without MF increased the End-Tidal CO 2 (etco 2 ) and fractional concentration of inspired co 2 (fico 2 ) at rest and on mild exertion, as expected. The use of the mask with MF brought FICO 2 levels comparably closer to baseline levels without the mask for both activities. The mask, with or without the MF, was found to be well fitting, comfortable and safe for use in children at rest and on mild exertion. The N95 mask tested offers a promising start for more studies in the paediatric population. Air pollution, such as haze or smog, is an evolving and increasingly significant problem around the world. A wide range of hazards of chronic air pollution in children include nocturnal cough, asthma, poor performance in neurobehavioral function, negative impact in cognitive development and harmful effects on brain development 1-5 . In particular, children represent a vulnerable segment of any population. They carry more risks of long term exposure to pollution over the course of their lives and are susceptible to acquiring chronic diseases in their developing lungs 6-11 . Use of masks and respirators can offer protection against air pollutants. However, the commercially available disposable particulate respirators, typically certified for surgical (which may only offer some barrier against larger particles) and occupational use, are mainly designed for and studied in adults. The test standards are specified according to adult breathing conditions and fit. There are to date, no masks designed for and evaluated in children. Several studies have investigated the effectiveness, safety, fit and comfort of different types of masks 12-15 . However these studies were done only in adult populations. Even alternatives such as cloth masks have been tested only in adult populations 16 . In another study, the facemasks for paediatric use (FPU, the masks that are not specifically designed for paediatric use but are the existing mask that may be used for children during emergency situation like that of airborne disease outbreaks) were tested mainly to evaluate the leakage associated with donning the FPU 17 . This study did show superiority of FPU in comparison to surgical masks in certain aspects, however, the study was not performed in children. One study was performed in children to evaluate the redesigned open system face mask. However, the objective of this study was to evaluate the mask for monitoring P ETCO2 during sedation in clinical practice and the children in this study donned the mask only for 30 sec. 18 . These and other similar studies merely point to the fact that there are no masks that are specifically designed and tested in children such that they can be prescribed for paediatric use in the setting of daily routine activities. In our study, the N95 masks were specifically designed for use in children and they were evaluated in children under conditions of routine daily activities. They are the first to be paired with a micro ventilator (micro fan, MF), designed to reduce the accumulation of exhaled carbon dioxide (CO 2 ), heat and humidity in the dead space of 
 Title: A randomised clinical trial to evaluate the safety, fit, comfort of a novel N95 mask in children

SOLUTION: False

PROBLEM: Paragraph: that can be specifically targeted by fusion-inhibitory peptides. Antiviral potency can be improved by sequence modification and lipid conjugation, and by adding linkers between the protein and lipid components. We exploit the uniquely broad spectrum antiviral activity of a parainfluenza F-derived peptide sequence that inhibits both parainfluenza and Nipah viruses, to investigate the influence of peptide orientation and intervening linker length on the peptides' interaction with transitional states of F, solubility, membrane insertion kinetics, and protease sensitivity. We assessed the impact of these features on biodistribution and antiviral efficacy in vitro and in vivo. The engineering approach based on biophysical parameters resulted in a peptide that is a highly effective inhibitor of both paramyxoviruses and a set of criteria to be used for engineering broad spectrum antivirals for emerging paramyxoviruses. Human parainfluenza viruses (HPIVs) are paramyxoviruses belonging to the respirovirus (HPIV1 and 3) or rubulavirus (HPIV2 and 4) genera that cause human respiratory diseases including bronchitis, bronchiolitis, and pneumonia in infants, children, or immune-compromised individuals. The HPIV species viruses are responsible for 30-40% of all acute respiratory tract infections in infants and children 1 . Nipah virus (NiV) is a zoonotic paramyxovirus of the henipavirus genus that represents a global health risk with broad, unpredictable pandemic potential. Infection with this virus is devastating, rapidly causing a generalized vasculitis leading to lethal encephalitis and serious respiratory infections. The common natural reservoirs of henipavirus genus members (including NiV, Hendra virus, Cedar virus and numerous newly identified species) are fruit bats 2,3 , but recent identification of rodent-origin henipa-like viruses that cause lethal respiratory disease in humans suggests that the range of natural mammalian hosts may be even broader 4 . Transmitted by air or food, its mechanism of infection is complex, and no drugs exist to prevent or treat infection. The recent human-to-human spread of NiV in Asia has raised the real possibility of global spread. NiV and HPIV, while different in their associated diseases and geography, infect using similar mechanisms and are vulnerable to the same antiviral strategy. Paramyxovirus infections are initiated by fusion between viral and host cell membranes. For HPIV3, NiV, and other paramyxoviruses, the surface glycoproteins play critical roles in the initial events of viral infection, mediating virion attachment to cells and fusion of the viral and cellular membranes. The viral fusion protein (F), upon insertion of the fusion peptide -formed after cleavage of the precursor F into its final fragment -into the host target cell membrane, forms a transient intermediate to pull the viral and cell membranes together. Two heptad-repeat regions that are present in each ectodomain of F refold to form a highly stable, antiparallel six-helix bundle structure that is coupled to membrane fusion. The structure required for this step can be specifically targeted by fusion-inhibitory peptides. The N-terminal repeat (HRN) is adjacent to the hydrophobic fusion peptide that inserts into the target cell membrane during the fusion process. The C-terminal repeat (HRC) immediately precedes the transmembrane domain. A folding-back of the F ectodomain drives the viral membrane towards the cell-associated fusion peptide to bring the two membranes into proximity, causing membrane fusion and viral entry. Peptides derived from the HRC of paramyxovirus F proteins interfere with formation of the six-helix bundle in a dominant-negative manner by binding to the transiently exposed HRN coiled coil in the transient fusion intermediate, thereby inhibiting membrane fusion 5 . We have shown the potential of modified fusion inhibitor peptides as NiV and HPIV antiviral agents, and showed that a sequence corresponding to the HRC domain of HPIV3 effectively inhibits both HPIV3 and NiV 6 . Interhelical packing interactions in the post-fusion core of the NiV and HPIV3 F proteins are important determinants of viral entry and its inhibition. Fusion inhibitor peptides can be engineered at the level of these parameters, for optimal inhibition, increasing potency for both viruses [6] [7] [8] [9] [10] . Conjugating cholesterol to a fusion inhibitor peptide enhances NiV antiviral activity up to 100-fold, by targeting the peptide to the plasma membrane where fusion occurs 8 and endows the fusion inhibitor with the ability to localize to the central nervous system, successfully preventing and treating NiV infection in a golden hamster model of disease 6 . Surprisingly, the most effective antiviral peptides for NiV and the related Hendra virus (HeV) are those derived from the F of HPIV3. The antiviral strategy discussed here exploits the uniquely broad spectrum antiviral activity of these HPIV3 derived inhibitory peptides to treat paramyxovirus infection. In an effort to understand the biophysical properties that correlate with peptide efficacy and thereby improve upon their antiviral utility, we explored biophysical features of the lipid-conjugated peptides that alter aggregation and membrane insertion kinetics. We have identified several properties that correlate with the peptides' potency and permit enhancement of antiviral effect for both HPIV3 and NiV. 
 Title: Broad spectrum antiviral activity for paramyxoviruses is modulated by biophysical properties of fusion inhibitory peptides Human paramyxoviruses include global causes of lower respiratory disease like the OPEN

SOLUTION:
True