scholarly journals Protein function Motif extraction based on single function category sequence alignment in yeast

2012 ◽  
Vol 8 (8) ◽  
pp. 1-9
Author(s):  
Khaled Ahmed
Keyword(s):  
Sequence Alignment ◽  
Protein Function ◽  
Single Function ◽  
Motif Extraction ◽  
Category Sequence

Prediction of Protein Function Using Ant Colony Sequence Alignment

2011 ◽  
Vol 8 (10) ◽  
pp. 2155-2158
Author(s):  
Qingguang Zeng ◽  
Bo Liao ◽  
Hao Liu ◽  
Dachao Li ◽  
Renfa Li
Keyword(s):  
Sequence Alignment ◽  
Protein Function ◽  
Ant Colony

scholarly journals An Application of the Eigenproblem for Biochemical Similarity

Symmetry ◽  
2021 ◽  
Vol 13 (10) ◽  
pp. 1849
Author(s):  
Dan-Marian Joiţa ◽  
Mihaela Aurelia Tomescu ◽  
Donatella Bàlint ◽  
Lorentz Jäntschi
Keyword(s):  
Amino Acids ◽  
Sequence Alignment ◽  
Protein Function ◽  
Scoring Function ◽  
Essential Amino Acids ◽  
Alignment Algorithm ◽  
Protein Alignment ◽  
Correct Alignment ◽  
Distance Matrices ◽  
Cartesian Coordinate

Protein alignment finds its application in refining results of sequence alignment and understanding protein function. A previous study aligned single molecules, making use of the minimization of sums of the squares of eigenvalues, obtained for the antisymmetric Cartesian coordinate distance matrices Dx and Dy. This is used in our program to search for similarities between amino acids by comparing the sums of the squares of eigenvalues associated with the Dx, Dy, and Dz distance matrices. These matrices are obtained by removing atoms that could lead to low similarity. Candidates are aligned, and trilateration is used to attach all previously striped atoms. A TM-score is the scoring function that chooses the best alignment from supplied candidates. Twenty essential amino acids that take many forms in nature are selected for comparison. The correct alignment is taken into account most of the time by the alignment algorithm. It was numerically detected by the TM-score 70% of the time, on average, and 15% more cases with close scores can be easily distinguished by human observation.

Reading the phosphorylation code: binding of the 14-3-3 protein to multivalent client phosphoproteins

2020 ◽  
Vol 477 (7) ◽  
pp. 1219-1225 ◽  
Author(s):  
Nikolai N. Sluchanko
Keyword(s):  
Protein Function ◽  
Intrinsically Disordered Protein ◽  
Structural Basis ◽  
Major Protein ◽  
Post Translational Modifications ◽  
Protein Protein Interaction ◽  
Intrinsically Disordered ◽  
Biochemical Journal ◽  
Multiple Binding ◽  
And Control

Many major protein–protein interaction networks are maintained by ‘hub’ proteins with multiple binding partners, where interactions are often facilitated by intrinsically disordered protein regions that undergo post-translational modifications, such as phosphorylation. Phosphorylation can directly affect protein function and control recognition by proteins that ‘read’ the phosphorylation code, re-wiring the interactome. The eukaryotic 14-3-3 proteins recognizing multiple phosphoproteins nicely exemplify these concepts. Although recent studies established the biochemical and structural basis for the interaction of the 14-3-3 dimers with several phosphorylated clients, understanding their assembly with partners phosphorylated at multiple sites represents a challenge. Suboptimal sequence context around the phosphorylated residue may reduce binding affinity, resulting in quantitative differences for distinct phosphorylation sites, making hierarchy and priority in their binding rather uncertain. Recently, Stevers et al. [Biochemical Journal (2017) 474: 1273–1287] undertook a remarkable attempt to untangle the mechanism of 14-3-3 dimer binding to leucine-rich repeat kinase 2 (LRRK2) that contains multiple candidate 14-3-3-binding sites and is mutated in Parkinson's disease. By using the protein-peptide binding approach, the authors systematically analyzed affinities for a set of LRRK2 phosphopeptides, alone or in combination, to a 14-3-3 protein and determined crystal structures for 14-3-3 complexes with selected phosphopeptides. This study addresses a long-standing question in the 14-3-3 biology, unearthing a range of important details that are relevant for understanding binding mechanisms of other polyvalent proteins.

The challenge of detecting modifications on proteins

2020 ◽  
Vol 64 (1) ◽  
pp. 135-153 ◽  
Author(s):  
Lauren Elizabeth Smith ◽  
Adelina Rogowska-Wrzesinska
Keyword(s):  
Mass Spectrometry ◽  
Protein Function ◽  
Chemical Properties ◽  
Lysine Acetylation ◽  
Mass Determination ◽  
Post Translational Modifications ◽  
Site Specific ◽  
The Common

Abstract Post-translational modifications (PTMs) are integral to the regulation of protein function, characterising their role in this process is vital to understanding how cells work in both healthy and diseased states. Mass spectrometry (MS) facilitates the mass determination and sequencing of peptides, and thereby also the detection of site-specific PTMs. However, numerous challenges in this field continue to persist. The diverse chemical properties, low abundance, labile nature and instability of many PTMs, in combination with the more practical issues of compatibility with MS and bioinformatics challenges, contribute to the arduous nature of their analysis. In this review, we present an overview of the established MS-based approaches for analysing PTMs and the common complications associated with their investigation, including examples of specific challenges focusing on phosphorylation, lysine acetylation and redox modifications.

Spatial localization of unknown proteins in the endoplasmic reticulum predicts functions

2007 ◽  
Vol 30 (4) ◽  
pp. 84
Author(s):  
Michael D. Jain ◽  
Hisao Nagaya ◽  
Annalyn Gilchrist ◽  
Miroslaw Cygler ◽  
John J.M. Bergeron
Keyword(s):  
Endoplasmic Reticulum ◽  
Protein Folding ◽  
Protein Synthesis ◽  
Protein Function ◽  
Protein Translocation ◽  
Spatial Localization ◽  
Predict Protein Function ◽  
Insight Into ◽  
Soluble Fractions ◽  
Er Membrane

Protein synthesis, folding and degradation functions are spatially segregated in the endoplasmic reticulum (ER) with respect to the membrane and the ribosome (rough and smooth ER). Interrogation of a proteomics resource characterizing rough and smooth ER membranes subfractionated into cytosolic, membrane, and soluble fractions gives a spatial map of known proteins involved in ER function. The spatial localization of 224 identified unknown proteins in the ER is predicted to give insight into their function. Here we provide evidence that the proteomics resource accurately predicts the function of new proteins involved in protein synthesis (nudilin), protein translocation across the ER membrane (nicalin), co-translational protein folding (stexin), and distal protein folding in the lumen of the ER (erlin-1, TMX2). Proteomics provides the spatial localization of proteins and can be used to accurately predict protein function.

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