Background The aim of this study was to evaluate the diagnostic value of C-reactive protein (CRP) test in detecting neonatal septicemia. Material/Methods We searched the Cochrane Library, PubMed, Springer, MBASE, Elsevier Science Direct, and Medline databases up to March 2017. To collect relevant data on CRP testing in patients with neonatal septicemia, we performed a meta-analysis of positive likelihood ratio (LR), sensitivity, negative LR, specificity and diagnostic odds ratio (dOR) of CRP testing, using Stata 12.0 and Meta-DiSc 1.4 data analysis software. Results Ten studies including 1819 participants were considered in this study. We found that positive LR, sensitivity, negative LR, specificity, and dOR of the CRP test for neonatal septicemia were 5.63 (95% CI=2.86 to 11.09), 0.70 (95% CI=0.66 to 0.75), 0.36 (95% CI=0.21 to 0.60), 0.89 (95% CI=0.87 to 0.91), and 17.99 (95% CI=6.50 to 49.83), respectively. The AUC and Q* index of this meta-analysis were 0.90 and 0.83, respectively. Conclusions The area under the curve (AUC), negative LR, positive LR, Q* index, specificity, and dOR of the CRP test suggest that it is appropriate for detecting neonatal septicemia.

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The effect of ratio and consecutive number of hydrophobic residues in the repeating unit of protein chains was investigated by MD simulation. The modified off-lattice HNP model was applied in this study. The protein chains constituted by different HNP ratios or different numbers of consecutively hydrophobic residues with the same chain length were simulated under a broad temperature range. We concluded that the proteins with higher ratio or larger number of sequentially hydrophobic residues present more orientated and compact structure under a certain low temperature. It is attributed to the lower non-bonded potential energy between H-H residual pairs, especially more hydrophobic residues in a procession among the protein chain. Considering the microscopic structure of the protein, more residue contacts are achieved with the proteins with higher ratios and sequential H residues under the low temperature. Meanwhile, with the ratio and consecutive number of H residues increasing, the distribution of stem length showed a transition from exponential decline to unimodal and even multiple peaks, indicating the specific ordered structure formed. These results provide an insight into 3D structural properties of proteins from their residue sequences, which has a primary structure at molecular level and, ultimately, a practical possibility of applying in biotechnological applications.