Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Protein Folding01:22

Protein Folding

Overview
Protein Folding01:25

Protein Folding

Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
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...
Protein Organization01:13

Protein Organization

Overview
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.

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Functional identification of 'hypothetical protein' structures with unknown function.

Journal of biomolecular structure & dynamics·2022
Same author

[Chordoma as a neurosurgical pathology].

Arkhiv patologii·2022
Same author

[Relationship between the Interhelical Packing Angles and the Length of α-Helices in Proteins].

Molekuliarnaia biologiia·2020
Same author

[Structure and Features of Amino Acid Sequences of L-Modules in SH3-Like Folds].

Molekuliarnaia biologiia·2019
Same author

Side projections of double-helical DNA: example of binding patterns of DNA in the complex with factor TFIIIA.

Journal of biomolecular structure & dynamics·2018
Same author

Chirality and Handedness of Protein Structures.

Biochemistry. Biokhimiia·2018

Related Experiment Video

Updated: Jun 5, 2026

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

Structures closed into cycles in proteins containing 3β-corners.

E A Boshkova1, A V Efimov

  • 1Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow Region, Russia.

Biochemistry. Biokhimiia
|December 21, 2010
PubMed
Summary

Protein structure growth pathways vary significantly. Closed structures like barrels are frequently formed early by adding beta-strands to the 3-beta-corner, indicating preferential usage of these routes.

More Related Videos

Self-assembly of Complex Two-dimensional Shapes from Single-stranded DNA Tiles
10:23

Self-assembly of Complex Two-dimensional Shapes from Single-stranded DNA Tiles

Published on: May 8, 2015

Analyzing and Building Nucleic Acid Structures with 3DNA
16:24

Analyzing and Building Nucleic Acid Structures with 3DNA

Published on: April 26, 2013

Related Experiment Videos

Last Updated: Jun 5, 2026

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

Self-assembly of Complex Two-dimensional Shapes from Single-stranded DNA Tiles
10:23

Self-assembly of Complex Two-dimensional Shapes from Single-stranded DNA Tiles

Published on: May 8, 2015

Analyzing and Building Nucleic Acid Structures with 3DNA
16:24

Analyzing and Building Nucleic Acid Structures with 3DNA

Published on: April 26, 2013

Area of Science:

  • Structural biology
  • Biophysics
  • Computational biology

Background:

  • Protein structure formation follows specific growth pathways.
  • Beta-proteins with 3-beta-corners represent a key structural motif.
  • Understanding these pathways is crucial for predicting protein folding and function.

Purpose of the Study:

  • To analyze the growth pathways of beta-protein structures.
  • To investigate the frequency of different structural formations from a root 3-beta-corner.
  • To examine amino acid sequence constraints in superhelix formation.

Main Methods:

  • Analysis of protein structural trees for beta-proteins.
  • Frequency analysis of completed protein structures within tree branches.
  • Examination of amino acid sequences and residue conformations at crossover sites.

Main Results:

  • Significant variation in the frequency of occurrence of known protein structures within the analyzed tree.
  • A high propensity (67%) for forming closed cyclic or barrel structures by adding 1-2 or 3 beta-strands to the root 3-beta-corner.
  • Identification of sterically constrained alpha(L)- or epsilon-conformations at crossover sites, favoring glycine or flexible residues.

Conclusions:

  • Protein structure growth pathways are not equally utilized; some are favored over others.
  • Early steps in beta-protein growth preferentially lead to closed structures.
  • Specific amino acid properties, like flexibility, are essential for accommodating steric constraints in superhelix formation.