This work developed a Chinese humor corpus containing 3,365 jokes collected from over 40 sources. Each joke was labeled with five levels of funniness, eight skill sets of humor, and six dimensions of intent by only one annotator. To validate the manual labels, we trained SVM (Support Vector Machine) and BERT (Bidirectional Encoder Representations from Transformers) with half of the corpus (labeled by one annotator) to predict the skill and intent labels of the other half (labeled by the other annotator). Based on two assumptions that a valid manually labeled corpus should follow, our results showed the validity for the skill and intent labels. As to the funniness label, the validation results showed that the correlation between the corpus label and user feedback rating is marginal, which implies that the funniness level is a harder annotation problem to be solved. The contribution of this work is two folds: 1) a Chinese humor corpus is developed with labels of humor skills, intents, and funniness, which allows machines to learn more intricate humor framing, effect, and amusing level to predict and respond in proper context (https://github.com/SamTseng/Chinese_Humor_MultiLabeled). 2) An approach to verify whether a minimum human labeled corpus is valid or not, which facilitates the validation of low-resource corpora.

During the production of our manuscript [1], an incorrect Figure ​Figure11 was put in place of the one we submitted, and we erred in not appropriately informing the production staff of this mistake. The corrected figure and the text describing this figure, as well as the figure legend, are present herein. Figure 1. Charge-Hydropathy plots. In (A) the IDP-Hydropathy scale was used, in (B) the Guy (1985) Hydropathy scale was used, and in (C) the Kyte-Doolittle (1981) hydropathy scale was used. Red circles indicate disordered proteins, blue circles indicate structured ... As stated in our manuscript [1], “The C-H plots generated using scale SVM parameters scale, Kyte-Doolittle hydropathy scale, and Guy hydropathy scale for whole protein prediction are shown in Figure ​Figure1.1. Figure ​Figure1A,1A, which is derived by SVM parameters scale, shows many fewer misclassified disordered proteins on the ordered side, compared to Figure ​Figure1B1B and ​and1C1C.” As further stated in reference [1]: “Figure 1. Charge-Hydropathy plots. In (A) the IDP-Hydropathy scale was used, in (B) the Guy (1985) Hydropathy scale was used, and in (C) the Kyte-Doolittle (1981) hydropathy scale was used. Red circles indicate disordered proteins, blue circles indicate structured proteins. For these plots, each scale was normalized to be in the interval of 0 to 1. The Guy’s scale is multiplied by -1 prior to normalization to conform to the energy rule set by Kyte-Doolittle scale. In (A) the function describing the boundary is:  = 3.31  -0.97. In (B) the function describing the boundary is:  = 2.32  -0.93. In (C), the function describing the boundary is  = 1.35  -0.49.” For more details, the reader is referred to the published manuscript [1].

BACKGROUND: The earliest whole protein order/disorder predictor (Uversky et al., Proteins, 41: 415-427 (2000)), herein called the charge-hydropathy (C-H) plot, was originally developed using the Kyte-Doolittle (1982) hydropathy scale (Kyte & Doolittle., J. Mol. Biol, 157: 105-132(1982)). Here the goal is to determine whether the performance of the C-H plot in separating structured and disordered proteins can be improved by using an alternative hydropathy scale. RESULTS: Using the performance of the CH-plot as the metric, we compared 19 alternative hydropathy scales, with the finding that the Guy (1985) hydropathy scale (Guy, Biophys. J, 47:61-70(1985)) was the best of the tested hydropathy scales for separating large collections structured proteins and intrinsically disordered proteins (IDPs) on the C-H plot. Next, we developed a new scale, named IDP-Hydropathy, which further improves the discrimination between structured proteins and IDPs. Applying the C-H plot to a dataset containing 109 IDPs and 563 non-homologous fully structured proteins, the Kyte-Doolittle (1982) hydropathy scale, the Guy (1985) hydropathy scale, and the IDP-Hydropathy scale gave balanced two-state classification accuracies of 79%, 84%, and 90%, respectively, indicating a very substantial overall improvement is obtained by using different hydropathy scales. A correlation study shows that IDP-Hydropathy is strongly correlated with other hydropathy scales, thus suggesting that IDP-Hydropathy probably has only minor contributions from amino acid properties other than hydropathy. CONCLUSION: We suggest that IDP-Hydropathy would likely be the best scale to use for any type of algorithm developed to predict protein disorder.

MOTIVATION: Molecular recognition features (MoRFs) are short binding regions located within longer intrinsically disordered regions that bind to protein partners via disorder-to-order transitions. MoRFs are implicated in important processes including signaling and regulation. However, only a limited number of experimentally validated MoRFs is known, which motivates development of computational methods that predict MoRFs from protein chains. RESULTS: We introduce a new MoRF predictor, MoRFpred, which identifies all MoRF types (α, β, coil and complex). We develop a comprehensive dataset of annotated MoRFs to build and empirically compare our method. MoRFpred utilizes a novel design in which annotations generated by sequence alignment are fused with predictions generated by a Support Vector Machine (SVM), which uses a custom designed set of sequence-derived features. The features provide information about evolutionary profiles, selected physiochemical properties of amino acids, and predicted disorder, solvent accessibility and B-factors. Empirical evaluation on several datasets shows that MoRFpred outperforms related methods: α-MoRF-Pred that predicts α-MoRFs and ANCHOR which finds disordered regions that become ordered when bound to a globular partner. We show that our predicted (new) MoRF regions have non-random sequence similarity with native MoRFs. We use this observation along with the fact that predictions with higher probability are more accurate to identify putative MoRF regions. We also identify a few sequence-derived hallmarks of MoRFs. They are characterized by dips in the disorder predictions and higher hydrophobicity and stability when compared to adjacent (in the chain) residues. AVAILABILITY: http://biomine.ece.ualberta.ca/MoRFpred/; http://biomine.ece.ualberta.ca/MoRFpred/Supplement.pdf.