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 Input:
Paragraph: The binding between peptide epitopes and major histocompatibility complex proteins (MHCs) is an important event in the cellular immune response. Accurate prediction of the binding between short peptides and the MHC molecules has long been a principal challenge for immunoinformatics. Recently, the modeling of MHC-peptide binding has come to emphasize quantitative predictions: instead of categorizing peptides as "binders" or "non-binders" or as "strong binders" and "weak binders", recent methods seek to make predictions about precise binding affinities. We developed a quantitative support vector machine regression (SVR) approach, called SVRMHC, to model peptide-MHC binding affinities. As a non-linear method, SVRMHC was able to generate models that out-performed existing linear models, such as the "additive method". By adopting a new "11-factor encoding" scheme, SVRMHC takes into account similarities in the physicochemical properties of the amino acids constituting the input peptides. When applied to MHC-peptide binding data for three mouse class I MHC alleles, the SVRMHC models produced more accurate predictions than those produced previously. Furthermore, comparisons based on Receiver Operating Characteristic (ROC) analysis indicated that SVRMHC was able to outperform several prominent methods in identifying strongly binding peptides. As a method with demonstrated performance in the quantitative modeling of MHCpeptide binding and in identifying strong binders, SVRMHC is a promising immunoinformatics tool with not inconsiderable future potential. 
 Title: Quantitative prediction of mouse class I MHC peptide binding affinity using support vector machine regression (SVR) models

Ex Output:
False


Ex Input:
Paragraph: As the lung is a portal between the ambient environment and the internal milieu, it is the most frequent site of serious infections. A number of factors predispose to pulmonary infection, and these include distortions in lung anatomy, decreased mucociliary clearance, as well as abnormal cellular and humoral immune responses. The optimal treatment of infection requires diagnosing its cause. As a large variety of microbes can infect the lung, and as the histopathology of noninfectious conditions frequently mimics infection, the differential diagnosis of pulmonary infection is often broad. While in many cases, the clinical history, radiographic findings, and the noninvasive sampling of secretions can establish the cause of infection, at times, a lung biopsy will be required. 
 Title: Pulmonary Infection

Ex Output:
False


Ex Input:
Paragraph: Posttranslational modifications (PTMs) of proteins include enzymatic changes by covalent addition of cellular regulatory determinants such as ubiquitin (Ub) and small ubiquitin-like modifier (SUMO) moieties. These modifications are widely used by eukaryotic cells to control the functional repertoire of proteins. Over the last decade, it became apparent that the repertoire of ubiquitiylation and SUMOylation regulating various biological functions is not restricted to eukaryotic cells, but is also a feature of human virus families, used to extensively exploit complex host-cell networks and homeostasis. Intriguingly, besides binding to host SUMO/Ub control proteins and interfering with the respective enzymatic cascade, many viral proteins mimic key regulatory factors to usurp this host machinery and promote efficient viral outcomes. Advanced detection methods and functional studies of ubiquitiylation and SUMOylation during virus-host interplay have revealed that human viruses have evolved a large arsenal of strategies to exploit these specific PTM processes. In this review, we highlight the known viral analogs orchestrating ubiquitin and SUMO conjugation events to subvert and utilize basic enzymatic pathways. Ubiquitinylation is an enzymatic cascade involving the covalent linkage of a small protein called ubiquitin to the amino group of a lysine residue in a substrate protein through an isopeptide bond to the C-terminal glycine of ubiquitin [5, 6] . Beside canonically transferring ubiquitin to a lysine residue, 
 Title: Viral Mimicry to Usurp Ubiquitin and SUMO Host Pathways

Ex Output:

False