scholarly journals In-silico characterization and structure-based functional annotation of a hypothetical protein from Campylobacter jejuni involved in propionate catabolism

2021 ◽  
Vol 19 (4) ◽  
pp. e43
Author(s):  
Lincon Mazumder ◽  
Mehedi Hasan ◽  
Ahmed Abu Rus'd ◽  
Mohammad Ariful Islam
Keyword(s):  
Campylobacter Jejuni ◽  
Protein Interactions ◽  
In Silico ◽  
Functional Annotation ◽  
3D Structure ◽  
Alpha Helix ◽  
Hypothetical Protein ◽  
Random Coil ◽  
Protein Protein Interactions ◽  
In Silico Characterization

Campylobacter jejuni is one of the most prevalent organisms associated with foodborne illness across the globe causing campylobacteriosis and gastritis. Many proteins of C. jejuni are still unidentified. The purpose of this study was to determine the structure and function of a non-annotated hypothetical protein (HP) from C. jejuni. A number of properties like physiochemical characteristics, 3D structure, and functional annotation of the HP (accession No. CAG2129885.1) were predicted using various bioinformatics tools followed by further validation and quality assessment. Moreover, the protein-protein interactions and active site were obtained from the STRING and CASTp server, respectively. The hypothesized protein possesses various characteristics including an acidic pH, thermal stability, water solubility, and cytoplasmic distribution. While alpha-helix and random coil structures are the most prominent structural components of this protein, most of it is formed of helices and coils. Along with expected quality, the 3D model has been found to be novel. This study has identified the potential role of the HP in 2-methylcitric acid cycle and propionate catabolism. Furthermore, protein-protein interactions revealed several significant functional partners. The in-silico characterization of this protein will assist to understand its molecular mechanism of action better. The methodology of this study would also serve as the basis for additional research into proteomic and genomic data for functional potential identification.

scholarly journals In-silico Structural Annotation of Methylthioadenosine Nucleosidase Protein Zm00014a_031618 in Maize (Zea mays L.)

2019 ◽  
pp. 1-8
Author(s):  
Gali Adamu Ishaku
Keyword(s):  
Zea Mays ◽  
In Silico ◽  
3D Structure ◽  
Alpha Helix ◽  
Random Coil ◽  
Chemical Parameters ◽  
Structural Annotation ◽  
In Silico Studies ◽  
Physical And Chemical Parameters ◽  
Physical And Chemical

Aims: The aim of this study was In-Silico structural annotation of an amino acid sequence of Methylthioadenosine Nucleosidase Protein Zm00014a_031618 in Maize (Zea mays) retrieved from NCBI with the accession number PWZ58979. Study Design: The use of In-Silico studies for the structural annotation of Methylthioadenosine Nucleosidase protein. Place and Duration of Study: The research was conducted at the Bioinformatics Laboratory, Chevron Biotechnology Centre, Modibbo Adama University of Yola, Nigeria. Between June 2018 to July 2018. Methodology: The Methylthioadenosine Nucleosidase protein was retrieved from NCBI, physical and chemical parameters were calculated using ExPASy - ProtParam tool, the server SOPMA was used for secondary structure analysis (helix, sheets, and coils) and I-TASSER was used to obtain the 3D structure. Results: ExPASy - Prot Param tool computated the various physical and chemical parameters such as molecular weight (MW) 30117.97, total number of positively (+R) 27, negatively charged residues (-R) 30, theoretical isoelectric point (pI) 5.96, aliphatic index (AI) 103.67 and grand average hydropathy (GRAVY) 0.293. The SOPMA server was used for calculating the secondary structural features of protein sequences as Alpha helix 39.16%, Extended strand 14.69%, Beta turn 6.64% and Random coil 39.51%. I-Tasser was used for predicting the 3D structure where 2qttA from PDB was used as the template. Conclusion: This study helped in understanding the structural analysis of the Methylthioadenosine Nucleosidase Protein Zm00014a_031618 in maize (Z. mays).

scholarly journals In Silico Functional Annotation of VP 128 Hypothetical Protein from Vibrio parahaemolyticus

10.4194/afs37 ◽  
2021 ◽  
Vol 1 (2) ◽  
Author(s):  
Moslema Jahan Mou ◽  
Sk Injamamul Islam ◽  
Sarower Mahfuj
Keyword(s):  
Protein Interactions ◽  
In Silico ◽  
Vibrio Parahaemolyticus ◽  
Active Sites ◽  
Three Dimensional ◽  
Hypothetical Protein ◽  
Physicochemical Characteristics ◽  
Dimensional Structure ◽  
Structural Domain ◽  
Protein Protein Interactions

Unknown or hypothetical proteins exist, but they have yet to be identified or correlated to gene sequences. Domains of unknown function are proteins that have been identified experimentally but do not have a known functional or structural domain. Using a variety of computational approaches and tools, this research investigated and characterized the likely functional characteristics of a hypothetical protein from Vibrio parahaemolyticus (Accession no. QOS18375.1). The physicochemical characteristics, subcellular localization, three-dimensional structure, protein-protein interactions, and functional elucidation of the protein are all available from this in silico perspective. Protein-protein interactions are investigated using the STRING software and resulted that VP128 putative protein interacts strongly with the GlpX type protein Fructose-1,6-bisphosphatase. The in-silico investigation documented the protein’s hydrophilic nature with predominantly alpha (α) helices in its secondary structure. Furthermore, the protein, according to the research, features a VP128 domain and is thought to bind ribosomal subunits and the top active sites of the model described also. Therefore, the research findings will facilitate the development of new antibacterial drugs against acute gastroenteritis and other serious diseases by providing a better knowledge of the role of VP128 domain.

NMR spectroscopy in the conformational analysis of peptides: an overview

2020 ◽  
Vol 27 ◽  
Author(s):  
Marian Vincenzi ◽  
Flavia Anna Mercurio ◽  
Marilisa Leone
Keyword(s):  
Nmr Spectroscopy ◽  
Protein Interactions ◽  
3D Structure ◽  
Theoretical Background ◽  
Triple Resonance ◽  
Protein Protein Interactions ◽  
Nmr Studies ◽  
Conformational Preferences ◽  
Dynamic Perspective ◽  
Nmr Methods

Background: NMR spectroscopy is one of the most powerful tools to study the structure and interaction properties of peptides and proteins from a dynamic perspective. Knowing the bioactive conformations of peptides is crucial in the drug discovery field to design more efficient analogue ligands and inhibitors of protein-protein interactions targeting therapeutically relevant systems. Objective: This review provides a toolkit to investigate peptide conformational properties by NMR. Methods: Articles cited herein, related to NMR studies of peptides and proteins were mainly searched through Pubmed and the web. More recent and old books on NMR spectroscopy written by eminent scientists in the field were consulted as well. Results: The review is mainly focused on NMR tools to gain the 3D structure of small unlabeled peptides. It is more application-oriented as it is beyond its goal to deliver a profound theoretical background. However, the basic principles of 2D homonuclear and heteronuclear experiments are briefly described. Protocols to obtain isotopically labeled peptides and principal triple resonance experiments needed to study them, are discussed as well. Conclusion: NMR is a leading technique in the study of conformational preferences of small flexible peptides whose structure can be often only described by an ensemble of conformations. Although NMR studies of peptides can be easily and fast performed by canonical protocols established a few decades ago, more recently we have assisted to tremendous improvements of NMR spectroscopy to investigate instead large systems and overcome its molecular weight limit.

In Silico Study of 1, 4 Alpha Glucan Branching Enzyme and Substrate Docking Studies

2020 ◽  
Vol 17 (1) ◽  
pp. 40-50
Author(s):  
Farzane Kargar ◽  
Amir Savardashtaki ◽  
Mojtaba Mortazavi ◽  
Masoud Torkzadeh Mahani ◽  
Ali Mohammad Amani ◽  
...  
Keyword(s):  
Phylogenetic Tree ◽  
In Silico ◽  
Alpha Helix ◽  
In Silico Analysis ◽  
Glycogen Storage ◽  
Docking Studies ◽  
Random Coil ◽  
Special Topic ◽  
Industrial Biotechnology ◽  
In Silico Study

Background: The 1,4-alpha-glucan branching protein (GlgB) plays an important role in the glycogen biosynthesis and the deficiency in this enzyme has resulted in Glycogen storage disease and accumulation of an amylopectin-like polysaccharide. Consequently, this enzyme was considered a special topic in clinical and biotechnological research. One of the newly introduced GlgB belongs to the Neisseria sp. HMSC071A01 (Ref.Seq. WP_049335546). For in silico analysis, the 3D molecular modeling of this enzyme was conducted in the I-TASSER web server. Methods: For a better evaluation, the important characteristics of this enzyme such as functional properties, metabolic pathway and activity were investigated in the TargetP software. Additionally, the phylogenetic tree and secondary structure of this enzyme were studied by Mafft and Prabi software, respectively. Finally, the binding site properties (the maltoheptaose as substrate) were studied using the AutoDock Vina. Results: By drawing the phylogenetic tree, the closest species were the taxonomic group of Betaproteobacteria. The results showed that the structure of this enzyme had 34.45% of the alpha helix and 45.45% of the random coil. Our analysis predicted that this enzyme has a potential signal peptide in the protein sequence. Conclusion: By these analyses, a new understanding was developed related to the sequence and structure of this enzyme. Our findings can further be used in some fields of clinical and industrial biotechnology.

scholarly journals Exploring Protein-Protein Interactions as Drug Targets for Anti-cancer Therapy with In Silico Workflows

2017 ◽  
pp. 221-236 ◽  
Author(s):  
Alexander Goncearenco ◽  
Minghui Li ◽  
Franco L. Simonetti ◽  
Benjamin A. Shoemaker ◽  
Anna R. Panchenko
Keyword(s):  
Cancer Therapy ◽  
Protein Interactions ◽  
In Silico ◽  
Drug Targets ◽  
Protein Protein Interactions ◽  
Anti Cancer

scholarly journals In Silico and In Vitro Studies on the Protein-Protein Interactions between Brugia malayi Immunomodulatory Protein Calreticulin and Human C1q

PLoS ONE ◽  
2014 ◽  
Vol 9 (9) ◽  
pp. e106413 ◽  
Author(s):  
Sunita Yadav ◽  
Smita Gupta ◽  
Chandrabose Selvaraj ◽  
Pawan Kumar Doharey ◽  
Anita Verma ◽  
...  
Keyword(s):  
Protein Interactions ◽  
In Silico ◽  
Brugia Malayi ◽  
In Vitro Studies ◽  
Protein Protein Interactions ◽  
Immunomodulatory Protein

scholarly journals Structural Model of the hUbA1-UbcH10 Quaternary Complex: In Silico and Experimental Analysis of the Protein-Protein Interactions between E1, E2 and Ubiquitin

PLoS ONE ◽  
2014 ◽  
Vol 9 (11) ◽  
pp. e112082 ◽  
Author(s):  
Stefania Correale ◽  
Ivan de Paola ◽  
Carmine Marco Morgillo ◽  
Antonella Federico ◽  
Laura Zaccaro ◽  
...  
Keyword(s):  
Protein Interactions ◽  
Experimental Analysis ◽  
In Silico ◽  
Structural Model ◽  
Protein Protein Interactions ◽  
Quaternary Complex

Furan warheads for covalent trapping of weak protein-protein interactions: cross-linking of thymosin β4 to actin

2021 ◽  
Author(s):  
Laia Miret Casals ◽  
Willem Vannecke ◽  
Kurt Hoogewijs ◽  
Gianluca Arauz ◽  
Marina Gay ◽  
...  
Keyword(s):  
Protein Interaction ◽  
Protein Interactions ◽  
3D Structure ◽  
Cross Linking ◽  
Thymosin Β4 ◽  
Protein Protein Interactions ◽  
Site Specific ◽  
Protein Protein Interaction ◽  
Covalent Trapping

We describe furan as a triggerable ‘warhead’ for site-specific cross-linking using the actin and thymosin β4 (Tβ4)-complex as model of a weak and dynamic protein-protein interaction with known 3D structure...

Protein-Protein Interactions (PPIs) as an Alternative to Targeting the ATP Binding Site of Kinase

2016 ◽  
pp. 249-277
Author(s):  
Sailu Sarvagalla ◽  
Mohane Selvaraj Coumar
Keyword(s):  
Protein Interactions ◽  
In Silico ◽  
Rational Design ◽  
Kinase Activity ◽  
Hot Spot ◽  
Binding Pocket ◽  
Atp Binding ◽  
Protein Protein Interactions ◽  
Structure Based Drug Design ◽  
Atp Binding Site

Most of the developed kinase inhibitor drugs are ATP competitive and suffer from drawbacks such as off-target kinase activity, development of resistance due to mutation in the ATP binding pocket and unfavorable intellectual property situations. Besides the ATP binding pocket, protein kinases have binding sites that are involved in Protein-Protein Interactions (PPIs); these PPIs directly or indirectly regulate the protein kinase activity. Of recent, small molecule inhibitors of PPIs are emerging as an alternative to ATP competitive agents. Rational design of inhibitors for kinase PPIs could be carried out using molecular modeling techniques. In silico tools available for the prediction of hot spot residues and cavities at the PPI sites and the means to utilize this information for the identification of inhibitors are discussed. Moreover, in silico studies to target the Aurora B-INCENP PPI sites are discussed in context. Overall, this chapter provides detailed in silico strategies that are available to the researchers for carrying out structure-based drug design of PPI inhibitors.

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