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".

Input: Consider Input: Paragraph: was first discovered in 2012. MERS-CoV can infect multiple host species and cause severe diseases in human. We conducted a series of phylogenetic and bioinformatic analyses to study the evolution dynamics of MERS-CoV among different host species with genomic data. Our analyses show: 1) 28 potential recombinant sequences were detected and they can be classified into seven potential recombinant types; 2) The spike (S) protein of MERS-CoV was under strong positive selection when Middle East Respiratory Syndrome coronavirus (MERS-CoV) is a novel beta-coronavirus with high pathogenicity, which imposes a serious threat to human health 1 . Substantial evidence has showed that MERS-CoVs have existed in central and east Africa for decades 2,3 , and have many natural hosts including two species of bats (Neoromicia capensis and Vespertilio superans), dromedary camel (Camelus dromedarius), and European hedgehog (Erinaceus europaeus) 4-7 . Yet it seemed that human MERS-CoV first isolated in Saudi Arabian in 2012, and then spread among humans worldwide 8 . Studies of prototype human MERS-CoV also suggested that the tMRCA (the time of most recent common ancestor) of human MERS-CoV can be traced back to about 2011 9 . Because the genome sequence of bat MERS-CoV is highly identical to that of human MERS-CoV, it has been indicated that human MERS-CoV might have a bat origin 10 , while there is also some evidence of camel-to-human MERS-CoV transmission 11,12 . Together, these studies proposed that zoonotic event may play a nontrivial part in MERS-CoV evolution and transmission. Previous studies showed that recombination was common among the members of beta-coronavirus 13,14 . By joining the previously unlinked DNA, recombination event can create new viral strains which may be capable of infecting new hosts and evading host's immuno-responses. The phylogenetic analysis showed that there were two main MERS-CoV clades-clade A and B, and clade B can be further divided into five phylogenetic groups 15 . There is evidence that recombination event had happened between group III and group V 15 . However, whether there was potential recombination event happened between the other groups or among multiple phylogenetic groups remains unclear. The genome of MERS-CoV is over 30,000 nucleotides (nt) in length, which contains seven predicted open reading frames (ORFs) and four structural genes-spike (S), envelope (E), membrane (M), and nucleocapsid (N) 16 (supplementary Fig. 1c ). The surface located spike (S) protein of beta-coronaviruses is one of the major determinants in their cross-species transmission because it mediates the virus-receptor recognition and thereby activates viral infection process 17 . Additionally, the receptor binding domain (RBD) on S protein's N-terminal is the key element for beta-coronavirus entering into host cells and the mutations in coronavirus's RBD affects its infection and cross-species capability 18, 19 . For example, the study of the spike protein from severe acute respiratory syndrome coronavirus (SARS-CoV), another beta-coronavirus with high pathogenicity, revealed four amino
Title: Evolutionary Dynamics of MERS- CoV: Potential Recombination, Positive Selection and Transmission OPEN

Output: False

Input: Consider Input: Paragraph: We have previously reported that the 3C-like proteinase of the coronavirus infectious bronchitis virus (IBV) is responsible for processing of the 1a and 1a/1b polyproteins to three mature products of 24, 10, and 100 kDa (Liu et al., 1994 (Liu et al., , 1997 Ng and Liu, 1998) . The C-terminal cleavage site of the 100-kDa protein was defined to be the Q 891(1b) -S 892(1b) dipeptide bond encoded by nucleotides 15, 129 to 15, 134 (Liu and Brown, 1995). In this report, other cleavage sites of the 3C-like proteinase in the polyprotein encoded by the ORF 1b region were mapped by coexpression, deletion, and site-directed mutagenesis studies. Using two ORF 1b-specific antisera, V58 and V17, three more Q-S(G) dipeptide bonds, encoded by nucleotides 16,929 to 16,934, 18,492 to 18,497, and 19,506 to 19,511, respectively, were demonstrated to be the cleavage sites of the 3C-like proteinase. Cleavage at these four positions would result in the release of four mature products with molecular masses of approximately 68, 58, 39, and 35 kDa. Among them, the 39-and 35-kDa proteins were specifically identified in IBV-infected cells. Taken together with the 100-kDa protein previously identified, these results suggest that the ORF 1b region of IBV mRNA1 may be able to encode five mature products.
Title: Proteolytic Mapping of the Coronavirus Infectious Bronchitis Virus 1b Polyprotein: Evidence for the Presence of Four Cleavage Sites of the 3C-like Proteinase and Identification of Two Novel Cleavage Products

Output: False

Input: Consider Input: Paragraph: RNA virus encodes a helicase essential for viral RNA transcription and replication when the genome size is larger than 7 kb. Coronavirus (CoV) has an exceptionally large RNA genome (~30 kb) and it encodes an essential replicase, the nonstructural protein 13 (nsp13), a member of superfamily 1 helicases. Nsp13 is among the evolutionary most conserved proteins not only in CoVs but also in nidovirales. Thus, it is considered as an important drug target. However, the high-resolution structure of CoV nsp13 remained unavailable even until more than a decade after the outbreak of the severe acute respiratory syndrome coronavirus (SARS-CoV) in 2003, which hindered the structure-based drug design. This is in part due to the intrinsic flexibility of nsp13. Here, we describe protocols of deducing the crystal structure of Middle East respiratory syndrome coronavirus (MERS-CoV) helicase in detail, which include protein expression, purification, crystallization, enzymatic characterization, and structure determination. With these methods, catalytically active recombinant MERS-CoV nsp13 protein can be prepared and crystallized and the crystal structure can be solved.
Title: Chapter 6 Deducing the Crystal Structure of MERS-CoV Helicase
Output: True