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Related Concept Videos

Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
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Conservation of Protein Domains02:26

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Base complementarity between the three base pairs of mRNA codon and the tRNA anticodon is not a failsafe mechanism. Inaccuracies can range from a single mismatch to no correct base pairing at all. The free energy difference between the correct and nearly correct base pairs can be as small as 3 kcal/ mol. With complementarity being the only proofreading step, the estimated error frequency would be one wrong amino acid in every 100 amino acids incorporated. However, error frequencies observed in...
Improving Translational Accuracy02:07

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Base complementarity between the three base pairs of mRNA codon and the tRNA anticodon is not a failsafe mechanism. Inaccuracies can range from a single mismatch to no correct base pairing at all. The free energy difference between the correct and nearly correct base pairs can be as small as 3 kcal/ mol. With complementarity being the only proofreading step, the estimated error frequency would be one wrong amino acid in every 100 amino acids incorporated. However, error frequencies observed in...

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Genetic Incorporation of Biosynthesized L-dihydroxyphenylalanine (DOPA) and Its Application to Protein Conjugation
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Genetic Incorporation of Biosynthesized L-dihydroxyphenylalanine (DOPA) and Its Application to Protein Conjugation

Published on: August 24, 2018

DOPA: GPU-based protein alignment using database and memory access optimizations.

Laiq Hasan1, Marijn Kentie, Zaid Al-Ars

  • 1Computer Engineering Laboratory, Faculty of Electrical Engineering Mathematics and Computer Science (EEMCS), Delft University of Technology (TU Delft), Mekelweg 4, 2628 CD, Delft, The Netherlands. l.hasan@tudelft.nl.

BMC Research Notes
|July 30, 2011
PubMed
Summary
This summary is machine-generated.

This study introduces Database Optimized Protein Alignment (DOPA), a GPU-accelerated method for faster and more accurate protein sequence alignment. DOPA optimizes database organization to significantly enhance computational performance.

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Area of Science:

  • Bioinformatics
  • Computational Biology
  • Genomics

Background:

  • The Smith-Waterman (S-W) algorithm provides optimal biological sequence alignment but is computationally intensive.
  • Existing heuristic methods like FASTA and BLAST offer speed at the expense of accuracy.
  • Growing sequence data necessitates efficient database restructuring for faster alignment.

Purpose of the Study:

  • To develop a high-performance protein sequence alignment implementation that overcomes the limitations of existing methods.
  • To accelerate the Smith-Waterman algorithm for practical applications in large-scale biological databases.

Main Methods:

  • Implementation of a novel protein sequence alignment algorithm on Graphics Processing Units (GPUs).
  • Optimization of database organization to minimize memory access and reduce bandwidth bottlenecks.
  • Development of the Database Optimized Protein Alignment (DOPA) system.

Main Results:

  • The DOPA implementation achieves a performance of 21.4 Giga Cell Updates Per Second (GCUPS).
  • This represents a 1.13-fold improvement over the previous fastest GPU-based implementation.
  • The optimized database organization effectively distributes workload across GPU multiprocessors.

Conclusions:

  • The DOPA system offers a significant performance enhancement for protein sequence alignment.
  • Organizing databases into equal-length sequence sets is key to efficient GPU utilization.
  • This GPU-based approach provides a faster and more accurate alternative for biological sequence analysis.