Multiple Protein Alignment

Multiple protein alignment is a computational method for arranging three or more amino acid sequences to identify conserved and variable regions, helping researchers infer shared ancestry and functional relationships. The process scores matches, substitutions, and gaps using substitution matrices and gap penalties, often aligning the most similar sequences first according to a guide tree before refining the combined alignment. In genetics, multiple protein alignment supports homology assessment, detection of conserved motifs and catalytic residues, prediction of structural or functional effects from mutations, and construction of evolutionary trees. These analyses connect sequence variation with protein function and guide comparative genomics and experimental research.

Multiple Protein Alignment - Related Videos

Research

JoVE Journal - Genetics

Demonstration of the Sequence Alignment to Predict Across Species Susceptibility Tool for Rapid Assessment of Protein Conservation

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Cited by 3 •

2023

Here, we present a protocol to utilize the latest version of the US Environmental Protection Agency Sequence Alignment to Predict Across Species Susceptibility (SeqAPASS) tool. This protocol demonstrates the application of the online tool to rapidly analyze protein conservation and provide customizable and easily interpretable predictions of chemical susceptibility across species.

Nuclear Magnetic Resonance Spectroscopy to Identify Multiple Phosphorylations in Proteins

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2025

This video demonstrates the use of nuclear magnetic resonance spectroscopy (NMR) techniques to identify multiple phosphorylations in a protein. The phosphorylation of a protein at specific amino acid causes the deshielding of the neighboring amide hydrogen, which generates the spectral difference.

Reverse Phase Protein Arrays Based Protein Expression Analysis: A Procedure for Simultaneous Quantification of Expression of Multiple Proteins from Cell Lysate

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2023

This video demonstrates the methodology for performing Reverse Phase Protein Arrays (RPPA) to study protein expression patterns from cell lysate. In RPPA, the lysate containing a mixture of proteins is printed on nitrocellulose slides and proteins of interest are analyzed using fluorescently labeled antibodies.

Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins

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Cited by 26 •

2016

We describe here a method to identify multiple phosphorylations of an intrinsically disordered protein by Nuclear Magnetic Resonance Spectroscopy (NMR), using Tau protein as a case study. Recombinant Tau is isotopically enriched and modified in vitro by a kinase prior to data acquisition and analysis.

Research

JoVE Journal - Biology
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Assembly, Loading, and Alignment of an Analytical Ultracentrifuge Sample Cell

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Cited by 21 •

2009

The analytical ultracentrifuge (AUC) sample cell holds sample and reference buffer and during experiments and is exposed to high vacuum and rotor speeds up to 60,000 rpm. This video will demonstrate the rigorous attention to detail necessary for assembly, loading and alignment of this very important component of an AUC experiment.

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