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 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.
Fischer Projections02:18

Fischer Projections

Learning to draw Fischer projections of molecules and understanding their relevance plays a crucial role in the visual depiction of organic molecules. A Fischer projection is a two-dimensional projection on a planar surface to simplify the three-dimensional wedge–dash representation of molecules. This is especially helpful in the case of molecules with multiple chiral centers that can be difficult to draw. Here, all the bonds of interest are represented as horizontal or vertical lines. While...
Protein Folding Quality Check in the RER01:29

Protein Folding Quality Check in the RER

ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
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.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...
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...

You might also read

Related Articles

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

Sort by
Same author

Implementation determinants and outcomes in the Philadelphia TelePrEP Program: a mixed methods study of client and staff perspectives.

Implementation science communications·2026
Same author

Addressing Pediatric COVID-19 Vaccine Hesitancy through Community Engagement: A Descriptive Evaluation of the VaxUpPhillyFamilies program.

Journal of pediatric nursing·2026
Same author

Lower self-efficacy and lower PrEP stigma predict telePrEP preferences among HIV self-testers.

Journal of acquired immune deficiency syndromes (1999)·2026
Same author

Protein language models accurately predict polymorphic peptide-modulated NK cell receptor-HLA class I interaction strengths.

Science advances·2026
Same author

Assessment of miRNAs as transcriptional regulators in respiratory syncytial virus infection through computational analysis and molecular docking studies.

PloS one·2026
Same author

Computational Analysis of GAT1 Mutations: Functional Consequences from Molecular Dynamics and Binding Free Energy Calculations.

International journal of molecular sciences·2025
Same journal

Protein sequence-similarity search acceleration using a heuristic algorithm with a sensitive matrix.

Journal of structural and functional genomics·2017
Same journal

Toward the next step in G protein-coupled receptor research: a knowledge-driven analysis for the next potential targets in drug discovery.

Journal of structural and functional genomics·2017
Same journal

Special issue: big data analyses in structural and functional genomics.

Journal of structural and functional genomics·2017
Same journal

Classification of ligand molecules in PDB with graph match-based structural superposition.

Journal of structural and functional genomics·2016
Same journal

VaProS: a database-integration approach for protein/genome information retrieval.

Journal of structural and functional genomics·2016
Same journal

NLDB: a database for 3D protein-ligand interactions in enzymatic reactions.

Journal of structural and functional genomics·2016
See all related articles

Related Experiment Video

Updated: Jun 3, 2026

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

Statistical measures on residue-level protein structural properties.

Yuanyuan Huang1, Stephen Bonett, Andrzej Kloczkowski

  • 1Program on Bioinformatics and Computational Biology, Iowa State University, Ames, IA 50014, USA. sunnyuan@iastate.edu

Journal of Structural and Functional Genomics
|April 1, 2011
PubMed
Summary
This summary is machine-generated.

This study statistically analyzes residue-level protein structures, revealing key distances and angles. These findings provide new insights into protein folding and structural analysis.

More Related Videos

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

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
14:55

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy

Published on: September 17, 2017

Related Experiment Videos

Last Updated: Jun 3, 2026

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

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
14:55

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy

Published on: September 17, 2017

Area of Science:

  • Protein structure analysis
  • Computational biology
  • Structural bioinformatics

Background:

  • Atomic-level protein structural properties are well-understood.
  • Residue-level properties (distances, angles) are crucial but less studied.
  • Experimental measurement of residue-level properties is challenging.

Purpose of the Study:

  • To statistically estimate and document residue-level protein structural properties.
  • To develop a software package for accessing these statistical data.
  • To investigate correlations between residue-level properties.

Main Methods:

  • Statistical analysis of known protein structures.
  • Development of a software package for data access.
  • Generation of residue-level statistical potentials.
  • Analysis of Ramachandran-like plots for correlated angles.

Main Results:

  • Statistical distributions and correlations of residue distances and angles were determined.
  • High probability ranges for these properties were identified, often linked to alpha-helices and beta-sheets.
  • Strong correlations among neighboring residue angles were revealed.
  • Applications in structural evaluation and refinement were demonstrated.

Conclusions:

  • Statistically derived residue-level properties offer systematic and quantitative assessments.
  • These properties provide insights into natural protein folding mechanisms.
  • The developed methods and data can supplement experimental findings in structure determination.