Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

What is Evolutionary History?

What is Evolutionary History?

Scientists record evolutionary history by analyzing fossil, morphological, and genetic data. The fossil record documents the history of life on Earth and provides evidence for evolution. However, both fossil and living organisms offer evidence that outlines Earth’s evolutionary history.

Protein and Protein Structure

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...

Structural Protein Function

Structural Protein Function

Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity. In bones and teeth, it mineralizes to...

Structural Protein Function

Structural Protein Function

Protein and Protein Structures

Protein and Protein Structures

Evolutionary Psychology

Evolutionary Psychology

Evolutionary psychology explores the origins of human behavior and mental processes by framing them within the context of natural selection, a theory famously propounded by Charles Darwin. This field asserts that many behaviors common across human societies — ranging from instinctive fear reactions to complex social interactions — arose as evolutionary adaptations. These adaptations enhanced the survival and reproductive success of our ancestors, thereby becoming embedded in the...

You might also read

Related Articles

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

Sort by

Same author

High-throughput machine learning-aided antibody discovery for cell surface antigens.

Cell systems·2026

Same author

In silico discovery of nanobody binders to a G-protein coupled receptor using AlphaFold-Multimer.

Nature communications·2026

Same author

Determinants of metal import and specificity in a bacterial transporter.

bioRxiv : the preprint server for biology·2026

Same author

The 2025 Westlake Autumn Symposium for Al Proteomics and Virtual Cell.

Genomics, proteomics & bioinformatics·2026

Same author

Machine learning enables efficient and effective affinity maturation of nanobodies.

bioRxiv : the preprint server for biology·2026

Same author

Machine learning reveals hidden dimensions of functional similarity in proteins.

Proceedings of the National Academy of Sciences of the United States of America·2026

Search research articles

Related Experiment Video

Updated: Jan 31, 2026

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR

Published on: December 16, 2013

Combining Evolutionary Covariance and NMR Data for Protein Structure Determination.

Yuanpeng Janet Huang¹, Kelly P Brock², Yojiro Ishida³

¹Center for Advanced Biotechnology and Medicine, Rutgers, The State University of New Jersey, Piscataway, NJ, United States; Department of Molecular Biology and Biochemistry, Rutgers, The State University of New Jersey, Piscataway, NJ, United States.

Methods in Enzymology

|January 7, 2019

Summary

Determining protein structures using Nuclear Magnetic Resonance (NMR) is difficult for large proteins. A new hybrid method combines evolutionary couplings (ECs) with sparse NMR data for more accurate 3D protein structure determination.

Keywords:

AutoStructure/ASDP Automated NMR data analysis Evolutionary couplings Hybrid methods Maximum entropy Multiple sequence alignment Protein NMR spectroscopy Protein families

More Related Videos

Identification of Disease-related Spatial Covariance Patterns using Neuroimaging Data

Identification of Disease-related Spatial Covariance Patterns using Neuroimaging Data

Published on: June 26, 2013

Crystallizing Membrane Proteins for Structure Determination using Lipidic Mesophases

Crystallizing Membrane Proteins for Structure Determination using Lipidic Mesophases

Published on: November 21, 2010

Related Experiment Videos

Last Updated: Jan 31, 2026

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR

Published on: December 16, 2013

Identification of Disease-related Spatial Covariance Patterns using Neuroimaging Data

Identification of Disease-related Spatial Covariance Patterns using Neuroimaging Data

Published on: June 26, 2013

Crystallizing Membrane Proteins for Structure Determination using Lipidic Mesophases

Crystallizing Membrane Proteins for Structure Determination using Lipidic Mesophases

Published on: November 21, 2010

Area of Science:

Biochemistry
Structural Biology
Biophysics

Background:

Solution-state Nuclear Magnetic Resonance (NMR) is limited for proteins >20kDa due to sparse and ambiguous data from extensive perdeuteration.
Evolutionary sequence information and covariance analysis offer reliable residue-residue contact data (evolutionary couplings, ECs).

Purpose of the Study:

To develop and validate a hybrid EC-NMR method for accurate 3D protein structure determination.
To improve structural accuracy and completeness compared to sparse NMR data alone.

Main Methods:

Combined evolutionary couplings (ECs) derived from sequence data with sparse NMR data.
Utilized backbone resonance assignments for small proteins and both backbone and sidechain methyl assignments for larger proteins.
Validated the EC-NMR method against X-ray crystallography and conventional NMR structures.

Main Results:

The EC-NMR method determined accurate and complete 3D protein structures.
Demonstrated the method's applicability to soluble proteins, with potential for solid-state NMR and membrane proteins.
Showed ECs can identify alternative protein conformational states.

Conclusions:

The hybrid EC-NMR approach overcomes limitations of traditional NMR for large proteins.
This method enhances structural determination accuracy and completeness.
EC-NMR offers a powerful tool for diverse protein structure studies and conformational analysis.