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".

[EX Q]: Paragraph: With concerns about the potential for the aerosol and airborne transmission of infectious agents, particularly influenza, more attention is being focused on the effectiveness of infection control procedures to prevent hospital-acquired infections by this route. More recently a number of different techniques have been applied to examine the temporalespatial information about the airflow patterns and the movement of related, suspended material within this air in a hospital setting. Closer collaboration with engineers has allowed clinical microbiologists, virologists and infection control teams to assess the effectiveness of hospital isolation and ventilation facilities. The characteristics of human respiratory activities have also been investigated using some familiar engineering techniques. Such studies aim to enhance the effectiveness of such preventive measures and have included experiments with humanlike mannequins using various tracer gas/particle techniques, real human volunteers with realtime non-invasive Schlieren imaging, numerical modelling using computational fluid dynamics, and small scale physical analogues with water. This article outlines each of these techniques in a non-technical manner, suitable for a clinical readership without specialist airflow or engineering knowledge. 
 Title: Observing and quantifying airflows in the infection control of aerosol-and airborne-transmitted diseases: an overview of approaches
[EX A]: True

[EX Q]: Paragraph: SARS-CoV-2, a member of the coronavirus family, is responsible for the current COVID-19 pandemic. We previously demonstrated that four nucleotide analogues (specifically, the active triphosphate forms of Sofosbuvir, Alovudine, AZT and Tenofovir alafenamide) inhibit the SARS-CoV-2 RNA-dependent RNA polymerase (RdRp). Tenofovir and emtricitabine are the two components in DESCOVY and TRUVADA, the two FDA-approved medications for use as pre-exposure prophylaxis (PrEP) to prevent HIV infection. This is a preventative method in which individuals who are HIV negative (but at high-risk of contracting the virus) take the combination drug daily to reduce the chance of becoming infected with HIV. PrEP can stop HIV from replicating and spreading throughout the body. We report here that the triphosphates of tenofovir and emtricitabine, the two components in DESCOVY and TRUVADA, act as terminators for the SARS-CoV-2 RdRp catalyzed reaction. These results provide a molecular basis to evaluate the potential of DESCOVY and TRUVADA as PrEP for COVID-19. 
 Title: Triphosphates of the Two Components in DESCOVY and TRUVADA are Inhibitors of the SARS-CoV-2 Polymerase
[EX A]: True

[EX Q]: Paragraph: The SARS 3C-like proteinase (SARS-3CLpro), which is the main proteinase of the SARS coronavirus, is essential to the virus life cycle. This enzyme has been shown to be active as a dimer in which only one protomer is active. However, it remains unknown how the dimer structure maintains an active monomer conformation. It has been observed that the Ser139-Leu141 loop forms a short 3 10 -helix that disrupts the catalytic machinery in the inactive monomer structure. We have tried to disrupt this helical conformation by mutating L141 to T in the stable inactive monomer G11A/R298A/Q299A. The resulting tetra-mutant G11A/L141T/R298A/Q299A is indeed enzymatically active as a monomer. Molecular dynamics simulations revealed that the L141T mutation disrupts the 3 10 -helix and helps to stabilize the active conformation. The coil-3 10 -helix conformational transition of the Ser139-Leu141 loop serves as an enzyme activity switch. Our study therefore indicates that the dimer structure can stabilize the active conformation but is not a required structure in the evolution of the active enzyme, which can also arise through simple mutations. 
 Title: Conformational Flexibility of a Short Loop near the Active Site of the SARS-3CLpro is Essential to Maintain Catalytic Activity OPEN
[EX A]:
True