instruction:
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".
question:
Paragraph: G-quadruplexes are non-canonical nucleic acid structures that control transcription, replication, and recombination in organisms. G-quadruplexes are present in eukaryotes, prokaryotes, and viruses. In the latter, mounting evidence indicates their key biological activity. Since data on viruses are scattered, we here present a comprehensive analysis of putative G-quadruplexes in the genome of all known viruses that can infect humans. We show that the presence, distribution, and location of G-quadruplexes are features characteristic of each virus class and family. Our statistical analysis proves that their presence within the viral genome is orderly arranged, as indicated by the possibility to correctly assign up to two-thirds of viruses to their exact class based on the G-quadruplex classification. For each virus we provide: i) the list of all G-quadruplexes formed by GG-, GGG-and GGGG-islands present in the genome (positive and negative strands), ii) their position in the viral genome along with the known function of that region, iii) the degree of conservation among strains of each G-quadruplex in its genome context, iv) the statistical significance of G-quadruplex formation. This information is accessible from a database 
 Title: G-quadruplex forming sequences in the genome of all known human viruses: a comprehensive guide Running title: Presence and conservation of G4s in human viruses
answer:
True


question:
Paragraph: Recent results have provided increasing evidence for the existence of an intermediate membrane compartment between the rough endoplasmic reticulum and the Golgi complex which seems to function in protein sorting and the regulation of membrane traffic in the early part of the exocytic pathway . Localization of resident marker proteins has shown that this compartment consists of both peripheral and central elements . The aim of the present review is to combine the data on the pre-Golgi compartment with previous ideas of membrane traffic at the ER-Golgi interface . We propose a model which describes how mobile, endosome-like elements of the pre-Golgi compartment function in the generation of the compositional andfunctional boundary between the widely distributed ER and the more central4 located Golgi stacks . 
 Title: Pathways of protein sorting and membrane traffic between the rough endoplasmic reticulum and the Golgi complex jaakko Saraste *t and Esa Kuismanent
answer:
True


question:
Paragraph: The protease domain within the RUBV (rubella virus) NS (non-structural) replicase proteins functions in the self-cleavage of the polyprotein precursor into the two mature proteins which form the replication complex. This domain has previously been shown to require both zinc and calcium ions for optimal activity. In the present study we carried out metal-binding and conformational experiments on a purified cysteine-rich minidomain of the RUBV NS protease containing the putative Zn 2+ -binding ligands. This minidomain bound to Zn 2+ with a stoichiometry of ≈0.7 and an apparent dissociation constant of < 500 nM. Fluorescence quenching and 8anilinonaphthalene-1-sulfonic acid fluorescence methods revealed that Zn 2+ binding resulted in conformational changes characterized by shielding of hydrophobic regions from the solvent. Mutational analyses using the minidomain identified residues Cys 1175 , Cys 1178 , Cys 1225 and Cys 1227 were required for the binding of Zn 2+ . Corresponding mutational analyses using a RUBV replicon confirmed that these residues were necessary for both proteolytic activity of the NS protease and viability. The present study demonstrates that the CXXC(X) 48 CXC Zn 2+ -binding motif in the RUBV NS protease is critical for maintaining the structural integrity of the protease domain and essential for proteolysis and virus replication. 
 Title: A cysteine-rich metal-binding domain from rubella virus non- structural protein is essential for viral protease activity and virus replication
answer:

False