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Related Concept Videos

Protein Organization01:24

Protein Organization

Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence.
Protein Organization01:13

Protein Organization

Overview
Globular and Fibrous Proteins02:21

Globular and Fibrous Proteins

Many proteins can be classified into two distinct subtypes - globular or fibrous. These two types differ in their shapes and solubilities.
Globular proteins are also known as spheroproteins and typically are approximately round in shape. They contain a mix of amino acid types and contain differing sequences in their primary structures. Globular proteins have many different functions, such as enzymes, cellular messengers, and molecular transporters. These roles often require the proteins to be...
Protein Folding01:22

Protein Folding

Overview
Protein and Protein Structure02:15

Protein and Protein Structure

Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme can...

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Related Experiment Video

Updated: Jun 12, 2026

Application of I TASSER, trRosetta, UCSF Chimera, HADDOCK server, and HEX loria for De Novo and In Silico Design of Proteins
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Application of I TASSER, trRosetta, UCSF Chimera, HADDOCK server, and HEX loria for De Novo and In Silico Design of Proteins

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DIALIGN-TX and multiple protein alignment using secondary structure information at GOBICS.

Amarendran R Subramanian1, Suvrat Hiran, Rasmus Steinkamp

  • 1Wilhelm-Schickard-Institut für Informatik, University of Tübingen, Sand 13, 72076 Tübingen, Germany.

Nucleic Acids Research
|May 26, 2010
PubMed
Summary
This summary is machine-generated.

We present new web tools for DIALIGN, enhancing multiple sequence alignment. These tools improve performance for related sequences and incorporate protein structure for better alignments.

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Last Updated: Jun 12, 2026

Application of I TASSER, trRosetta, UCSF Chimera, HADDOCK server, and HEX loria for De Novo and In Silico Design of Proteins
05:08

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A Protocol for Computer-Based Protein Structure and Function Prediction
16:41

A Protocol for Computer-Based Protein Structure and Function Prediction

Published on: November 3, 2011

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web
09:51

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web

Published on: July 16, 2017

Area of Science:

  • Bioinformatics
  • Computational Biology
  • Sequence Analysis

Background:

  • Multiple sequence alignment is crucial for understanding protein function and evolution.
  • Existing alignment tools may have limitations with diverse sequence relationships or structural information.

Purpose of the Study:

  • To introduce user-friendly web interfaces for two advanced DIALIGN multiple sequence alignment program extensions.
  • To enhance the capabilities of DIALIGN for analyzing both globally and locally related sequence sets.
  • To integrate protein secondary structure information into the multiple alignment process.

Main Methods:

  • DIALIGN-TX combines greedy and progressive alignment heuristics.
  • A novel DIALIGN version utilizes predicted protein secondary structures alongside primary sequences.
  • Web interfaces were developed and made accessible via the Göttingen Bioinformatics Compute Server (GOBICS).

Main Results:

  • DIALIGN-TX demonstrates improved performance on varied sequence sets.
  • The structure-aware DIALIGN version facilitates more accurate protein alignments.
  • Web-based access to these advanced alignment tools is now available.

Conclusions:

  • The new web interfaces provide enhanced tools for multiple sequence alignment.
  • These extensions offer improved accuracy and flexibility for bioinformatics research.
  • The integration of structural information represents a significant advancement in alignment methodology.