Journal of Theoretical & Computational Chemistry最新文献_第5页

In vitro Acetylcholinesterase inhibitory activity of polyphenolic compounds identified from Matricaria recutita 苦参多酚类化合物体外乙酰胆碱酯酶抑制活性的研究

IF 2.4

Journal of Theoretical & Computational Chemistry Pub Date : 2020-09-13 DOI: 10.1142/s0219633620500297

S. W. Qader, H. Abdallah, Mstaffa Zahid, L. S. Chua

引用次数: 1

Computational Studies of 3D-QSAR on a Highly Active Series of Naturally Occurring Non-Nucleoside Inhibitors of HIV-1 RT (NNRTI) 一系列高活性HIV-1RT天然非核苷抑制剂（NNRTI）的3D-QSAR计算研究

IF 2.4

Journal of Theoretical & Computational Chemistry Pub Date : 2020-09-09 DOI: 10.1142/s0219633620500364

Waqar Hussain, Arshia Majeed, A. Akhtar, N. Rasool

引用次数: 0

Insights into the binding of dorzagliatin with glucokinase: A molecular dynamics simulation 多唑菌素与葡萄糖激酶结合的分子动力学模拟

IF 2.4

Journal of Theoretical & Computational Chemistry Pub Date : 2020-09-04 DOI: 10.1142/s0219633620500273

Wei Liu, Chenhui Yao, Qian Shang, Yuqiang Liu, Changying Liu, Fancui Meng

引用次数: 4

Extrapolation in quantum chemistry: Insights on energetics and reaction dynamics 量子化学中的外推：对能量学和反应动力学的见解

IF 2.4

Journal of Theoretical & Computational Chemistry Pub Date : 2020-09-02 DOI: 10.1142/s0219633620300013

A. Varandas

引用次数: 5

Computational chemistry methods to investigate the effects caused by DNA variants linked with disease 计算化学方法研究与疾病相关的DNA变异所造成的影响

IF 2.4

Journal of Theoretical & Computational Chemistry Pub Date : 2020-09-01 DOI: 10.1142/s0219633619300015

Mahesh Koirala, E. Alexov

引用次数: 2

Studies on the structure and conformational flexibility of secondary structures in amyloid beta — A quantum chemical study 淀粉样蛋白二级结构的结构和构象柔韧性研究-量子化学研究

IF 2.4

Journal of Theoretical & Computational Chemistry Pub Date : 2020-09-01 DOI: 10.1142/s0219633620500145

M. Ganesan, S. Paranthaman

{"title":"Studies on the structure and conformational flexibility of secondary structures in amyloid beta — A quantum chemical study","authors":"M. Ganesan, S. Paranthaman","doi":"10.1142/s0219633620500145","DOIUrl":"https://doi.org/10.1142/s0219633620500145","url":null,"abstract":"Density functional theory (DFT) calculations are performed to study the conformational flexibility of secondary structures in amyloid beta (A[Formula: see text]) polypeptide. In DFT, M06-2X/6-31[Formula: see text]G(d, p) method is used to optimize the secondary structures of 2LFM and 2BEG in gas phase and in solution phase. Our calculations show that the secondary structures are energetically more stable in solution phase than in gas phase. This is due to the presence of strong solvent interaction with the secondary structures considered in this study. Among the backbone [Formula: see text] and [Formula: see text] dihedral angles, [Formula: see text] varies significantly in sheet structure. This is due to the absence of intermolecular hydrogen bond (H-bond) interactions in sheets considered in this study. Our calculations show that the conformational transition of helix/coil to sheet or vice-versa is due to the floppiness of the amino acid residues. This is observed from the Ramachandran map of the studied secondary structures. Further, it is noted that the intramolecular H-bond interactions play a significant role in the conformational transition of secondary structures of A[Formula: see text].","PeriodicalId":49976,"journal":{"name":"Journal of Theoretical & Computational Chemistry","volume":null,"pages":null},"PeriodicalIF":2.4,"publicationDate":"2020-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1142/s0219633620500145","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"42604933","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 3

Editorial: Special Issue on Computational Chemistry and Diseases 社论：计算化学与疾病特刊

IF 2.4

Journal of Theoretical & Computational Chemistry Pub Date : 2020-09-01 DOI: 10.1142/s0219633620020034

Minghui Li

引用次数: 0

Computational analysis of hereditary spastic paraplegia mutations in the kinesin motor domains of KIF1A and KIF5A KIF1A和KIF5A运动蛋白结构域遗传性痉挛性截瘫突变的计算分析

IF 2.4

Journal of Theoretical & Computational Chemistry Pub Date : 2020-09-01 DOI: 10.1142/s0219633620410035

Vidhyanand Mahase, Adebiyi Sobitan, C. Johnson, Farion Cooper, Yixin Xie, Lin Li, S. Teng

{"title":"Computational analysis of hereditary spastic paraplegia mutations in the kinesin motor domains of KIF1A and KIF5A","authors":"Vidhyanand Mahase, Adebiyi Sobitan, C. Johnson, Farion Cooper, Yixin Xie, Lin Li, S. Teng","doi":"10.1142/s0219633620410035","DOIUrl":"https://doi.org/10.1142/s0219633620410035","url":null,"abstract":"Hereditary spastic paraplegias (HSPs) are a genetically heterogeneous collection of neurodegenerative disorders categorized by progressive lower-limb spasticity and frailty. The complex HSP forms are characterized by various neurological features including progressive spastic weakness, urinary sphincter dysfunction, extra pyramidal signs and intellectual disability (ID). The kinesin superfamily proteins (KIFs) are microtubule-dependent molecular motors involved in intracellular transport. Kinesins directionally transport membrane vesicles, protein complexes, and mRNAs along neurites, thus playing important roles in neuronal development and function. Recent genetic studies have identified kinesin mutations in patients with HSPs. In this study, we used the computational approaches to investigate the 40 missense mutations associated with HSP and ID in KIF1A and KIF5A. We performed homology modeling to construct the structures of kinesin–microtubule binding domain and kinesin–tubulin complex. We applied structure-based energy calculation methods to determine the effects of missense mutations on protein stability and protein–protein interaction. The results revealed that the most of disease-causing mutations could change the folding free energy of kinesin motor domain and the binding free energy of kinesin–tubulin complex. We found that E253K associated with ID in KIF1A decrease the protein stability of kinesin motor domains. We showed that the HSP mutations located in kinesin–tubulin complex interface, such as K253N and R280C in KIF5A, can destabilize the kinesin–tubulin complex. The computational analysis provides useful information for understanding the roles of kinesin mutations in the development of ID and HSPs.","PeriodicalId":49976,"journal":{"name":"Journal of Theoretical & Computational Chemistry","volume":null,"pages":null},"PeriodicalIF":2.4,"publicationDate":"2020-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1142/s0219633620410035","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"47152518","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 2

Theoretical elucidation of the energy conversion rate in organic photovoltaic cells of the fullerene nanostructure derivatives. A density functional theory study 富勒烯纳米结构衍生物在有机光伏电池中能量转换率的理论阐明。密度泛函理论研究

IF 2.4

Journal of Theoretical & Computational Chemistry Pub Date : 2020-08-19 DOI: 10.1142/s021963362050025x

Nadjet Deddouche, H. Chemouri

引用次数: 0

Study on the mechanism of furfural to maleic acid oxidized by hydrogen peroxide in formic acid solution 甲酸溶液中过氧化氢氧化糠醛制马来酸的机理研究

IF 2.4

Journal of Theoretical & Computational Chemistry Pub Date : 2020-08-01 DOI: 10.1142/s0219633620500194

Aiyun Hu, Xinzhi Wang, Xiang Wang, Qingrui Peng, Haijun Wang

{"title":"Study on the mechanism of furfural to maleic acid oxidized by hydrogen peroxide in formic acid solution","authors":"Aiyun Hu, Xinzhi Wang, Xiang Wang, Qingrui Peng, Haijun Wang","doi":"10.1142/s0219633620500194","DOIUrl":"https://doi.org/10.1142/s0219633620500194","url":null,"abstract":"Although the conversion of furfural to formic acid oxidized by H2O2 in formic acid is very high, the molecular mechanism remains unknown. This work describes the entire reaction process of the condensation reaction based on the density functional theory (DFT). It is found that H acts as a shuttle throughout most of the basic reaction steps during this transformation. Besides, Baeyer–Villiger oxidation and Baeyer–Villiger rearrangement are also discovered during this process with the opening of furan ring following afterward. The reactants, products and intermediates in the reaction process are optimized; all possible reaction paths are considered as well as the energy barriers to be overcome at each step. Thermochemical data concerned with the conversion of furfural to maleic acid showed that the maximum energy barrier at 378.15[Formula: see text]K was 39.83[Formula: see text]kcal/mol. The results of this study do not only correspond with the existing conclusions about the reaction in question from previous research but also supplement to the study of the pathways and mechanisms of the reaction, which can provide reference and guidance for further research, both experimentally and theoretically.","PeriodicalId":49976,"journal":{"name":"Journal of Theoretical & Computational Chemistry","volume":null,"pages":null},"PeriodicalIF":2.4,"publicationDate":"2020-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1142/s0219633620500194","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"41713734","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 2