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

Conserved Binding Sites01:49

Conserved Binding Sites

4.1K
Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...
4.1K
Protein Folding01:22

Protein Folding

116.8K
Overview
116.8K
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

7.8K
Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
7.8K
Spin–Spin Coupling: Three-Bond Coupling (Vicinal Coupling)01:22

Spin–Spin Coupling: Three-Bond Coupling (Vicinal Coupling)

1.0K
Vicinal or three-bond coupling is commonly observed between protons attached to adjacent carbons. Here, nuclear spin information is primarily transferred via electron spin interactions between adjacent C‑H bond orbitals. This generally favors the antiparallel arrangement of spins, so 3J values are usually positive.
The extent of coupling depends on the C‑C bond length, the two H‑C‑C angles, any electron-withdrawing substituents, and the dihedral angle between the...
1.0K
Spin–Spin Coupling: One-Bond Coupling01:17

Spin–Spin Coupling: One-Bond Coupling

912
Coupling interactions are strongest between NMR-active nuclei bonded to each other, where spin information can be transmitted directly through the pair of bonding electrons. While nuclei polarize their electrons to the opposite spins, the bonding electron pair has opposite spins. Configurations with antiparallel nuclear spins are expected to be lower in energy. When coupling makes antiparallel states more favorable, J is considered to have a positive value. The one-bond coupling constant, 1J,...
912
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

2.5K
Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order...
2.5K

You might also read

Related Articles

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

Sort by
Same author

Corrigendum to "<sup>19</sup>F NMR Strategy for Probing Site-specific RNA Dynamics in Large RNA-protein Complexes: Application to the Hfq RNA Chaperone" [J. Mol. Biol. 438 (2026) 169797].

Journal of molecular biology·2026
Same author

Aromatic Residues in Mobile Regions Distal to the Active Site Support the Closed Conformation of <i>E. coli</i> DXPS.

Biochemistry·2026
Same author

<sup>19</sup>F NMR Strategy for Probing Site-specific RNA Dynamics in Large RNA-protein Complexes: Application to the Hfq RNA Chaperone.

Journal of molecular biology·2026
Same author

Sulfur partitioning from cysteine controls T cell proliferation and effector function.

Cell·2026
Same author

Distinct control of T cell proliferation and effector function by partitioning of intracellular sulfur from cysteine.

bioRxiv : the preprint server for biology·2026
Same author

Aromatic residues in mobile regions distal to the active site support the closed conformation of <i>E. coli</i> DXPS.

bioRxiv : the preprint server for biology·2025
Same journal

The Role of Functional Groups in Substituted Benzoic Acids Used as Dopants in Liquid Crystal Mixtures on the Nematic-Isotropic Transitions.

The journal of physical chemistry. B·2026
Same journal

Hyperfine Coupling Quantifies Hole Delocalization in Triarylamine Radical Cations of D-χ-A Molecules.

The journal of physical chemistry. B·2026
Same journal

A Solvatochromic-Chemometric Framework to Resolve Subtle Polarity Microenvironment Differences in Cycloalkanes Driven by Molecular Conformation and Substituent Effects: A Proof-Of-Concept for Advanced Aviation Fuel Design.

The journal of physical chemistry. B·2026
Same journal

Selective Effects of Backbone Cyclization and Disulfide Bonding as Global Covalent Constraints on the Conformational Ensemble of Sunflower Trypsin Inhibitor-1.

The journal of physical chemistry. B·2026
Same journal

Europium Coordination Structure in Peptide Complexes Resolved with Simulation and X-ray Absorption Spectroscopy.

The journal of physical chemistry. B·2026
Same journal

Competitive Coordination and Structural Evolution of Phenylalanine-Mg<sup>2+</sup> Complexes in Microaqueous Environments: Insights from DFT and Molecular Dynamics Simulations.

The journal of physical chemistry. B·2026
See all related articles

Related Experiment Video

Updated: May 16, 2025

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues
07:08

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues

Published on: July 14, 2015

7.2K

Thermodynamic Coupling in a Consensus-Designed Spectrin Repeat Protein.

Mark Petersen1, Soumya Prakash Behera1, Ananya Majumdar2

  • 1The T.C. Jenkins Department of Biophysics, Johns Hopkins University, 3400 N. Charles St., Baltimore, Maryland 21218, United States.

The Journal of Physical Chemistry. B
|May 5, 2025
PubMed
Summary
This summary is machine-generated.

This study quantifies protein folding cooperativity in spectrin repeat arrays. Consensus sequences enhanced stability, revealing helical propagation drives cooperative folding in these repeat proteins.

More Related Videos

Purification and Reconstitution of TRPV1 for Spectroscopic Analysis
11:53

Purification and Reconstitution of TRPV1 for Spectroscopic Analysis

Published on: July 3, 2018

7.9K
Transmembrane Domain Oligomerization Propensity determined by ToxR Assay
06:45

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay

Published on: May 26, 2011

15.2K

Related Experiment Videos

Last Updated: May 16, 2025

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues
07:08

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues

Published on: July 14, 2015

7.2K
Purification and Reconstitution of TRPV1 for Spectroscopic Analysis
11:53

Purification and Reconstitution of TRPV1 for Spectroscopic Analysis

Published on: July 3, 2018

7.9K
Transmembrane Domain Oligomerization Propensity determined by ToxR Assay
06:45

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay

Published on: May 26, 2011

15.2K

Area of Science:

  • Protein folding thermodynamics
  • Structural biology
  • Biophysics

Background:

  • Cooperativity is crucial for protein folding and design.
  • Repeat proteins, like spectrin, are model systems for studying folding cooperativity.
  • Spectrin repeats possess a unique elongated alpha-helix spanning adjacent repeats.

Purpose of the Study:

  • To quantify the cooperativity of folding in spectrin repeat arrays using a consensus approach.
  • To investigate the structural and thermodynamic basis of cooperativity in spectrin repeats.
  • To determine the role of helical propagation in the cooperative folding of spectrin repeat arrays.

Main Methods:

  • Generating and characterizing consensus spectrin repeat sequences.
  • Utilizing Circular Dichroism (CD) and Nuclear Magnetic Resonance (NMR) spectroscopy for structural analysis.
  • Employing an Ising model to analyze the unfolding thermodynamics of single and tandem repeats.

Main Results:

  • A consensus spectrin repeat sequence was generated, exhibiting enhanced stability compared to extant repeats.
  • Tandem pairs of consensus spectrin repeats showed further stabilization, confirming cooperative effects.
  • Increased stability was attributed to intrinsic, not interfacial, stabilization within the repeats.
  • Helical propagation was identified as the primary driver of cooperativity, with a secondary role in stabilizing partially folded states.

Conclusions:

  • Consensus spectrin repeat sequences are more stable and demonstrate cooperative folding.
  • Helical propagation is the key mechanism underlying cooperativity in spectrin repeat arrays.
  • Understanding this cooperativity is vital for protein design and predicting protein behavior.