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

Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

8.7K
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...
8.7K
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

3.0K
3.0K
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

2.6K
2.6K
Cooperative Binding of Transcription Regulators02:13

Cooperative Binding of Transcription Regulators

7.2K
Transcriptional regulators bind to specific cis-regulatory sequences in the DNA to regulate gene transcription. These cis-regulatory sequences are very short, usually less than ten nucleotide pairs in length. The short length means that there is a high probability of the exact same sequence randomly occurring throughout the genome.  Since regulators can also bind to groups of similar sequences, this further increases the chances of random binding. Transcriptional regulators form...
7.2K
Cooperative Binding of Transcription Regulators02:13

Cooperative Binding of Transcription Regulators

2.5K
2.5K
Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

19.3K
Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
19.3K

You might also read

Related Articles

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

Sort by
Same author

American science at 250.

Science (New York, N.Y.)·2026
Same author

Structure of a sparsely populated chimeric intermediate that facilitates fold-switching of a metamorphic protein.

bioRxiv : the preprint server for biology·2026
Same author

Oligomerization of PER2 as a dynamic mode of regulation of the mammalian circadian clock.

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

Selective control of ligand binding through a distal mutation that alters the protein native ensemble.

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

Morpheus: a fragment-based algorithm to predict fold-switching behaviour in proteins across proteomes.

Bioinformatics (Oxford, England)·2025
Same author

Local and Global Breathing Motions Prime the Access to Buried Binding Site in an Antibiotic-Sequestering Protein.

ACS bio & med chem Au·2025
Same journal

Aromatic Cage-Directed Azide-Methyllysine Photochemistry for Profiling Nonhistone Interacting Partners of the MeCP2 Methyl-CpG-Binding Domain.

Biochemistry·2026
Same journal

Differential Hydroxypyruvate Processing by <i>E. coli</i> and <i>P. aeruginosa</i> DXP Synthases Reveals Preferential Xylulose 5-Phosphate Formation by the <i>P. aeruginosa</i> Enzyme.

Biochemistry·2026
Same journal

Structural and Functional Characterization of Heterologous Nitrogenase Complexes.

Biochemistry·2026
Same journal

Discovery of Bacterial Unspecific Peroxygenases.

Biochemistry·2026
Same journal

Lactate Biology: Subcellular Routing and Chemical Form Define Function.

Biochemistry·2026
Same journal

Nature's Anaerobic Toolkit: Glycyl Radical Enzymes and Their Expanding Functional and Mechanistic Diversity.

Biochemistry·2026
See all related articles

Related Experiment Video

Updated: Jan 26, 2026

Engineering Cell-permeable Protein
21:08

Engineering Cell-permeable Protein

Published on: December 28, 2009

15.0K

Engineering Order and Cooperativity in a Disordered Protein.

Sneha Munshi1, Sandhyaa Subramanian1, Samyuktha Ramesh1

  • 1Department of Biotechnology, Bhupat & Jyoti Mehta School of Biosciences , Indian Institute of Technology Madras , Chennai 600036 , India.

Biochemistry
|April 20, 2019
PubMed
Summary
This summary is machine-generated.

Hydrophobic mutations can induce structural order and stability in disordered proteins, revealing emergent properties of protein folding and function. These findings highlight non-additive hydrophobic effects in protein evolution and design.

More Related Videos

ECM Protein Nanofibers and Nanostructures Engineered Using Surface-initiated Assembly
16:33

ECM Protein Nanofibers and Nanostructures Engineered Using Surface-initiated Assembly

Published on: April 17, 2014

13.0K
Protein Engineering by Yeast Surface Display
05:49

Protein Engineering by Yeast Surface Display

Published on: November 29, 2024

3.5K

Related Experiment Videos

Last Updated: Jan 26, 2026

Engineering Cell-permeable Protein
21:08

Engineering Cell-permeable Protein

Published on: December 28, 2009

15.0K
ECM Protein Nanofibers and Nanostructures Engineered Using Surface-initiated Assembly
16:33

ECM Protein Nanofibers and Nanostructures Engineered Using Surface-initiated Assembly

Published on: April 17, 2014

13.0K
Protein Engineering by Yeast Surface Display
05:49

Protein Engineering by Yeast Surface Display

Published on: November 29, 2024

3.5K

Area of Science:

  • Biochemistry
  • Structural Biology
  • Protein Folding

Background:

  • Protein structural disorder results from hydrophobic and electrostatic interactions.
  • The hydrophobic effect's role in protein native states is complex due to entropic and energetic compensation.
  • Understanding protein order in disordered systems is crucial for protein design.

Purpose of the Study:

  • To investigate how hydrophobic substitutions influence structural order and cooperativity in disordered proteins.
  • To explore the emergent properties of protein folding and function upon engineering mutations.
  • To provide experimental evidence for the role of non-additive hydrophobic effects.

Main Methods:

  • Sequence-structure analysis.
  • Equilibrium and kinetic spectroscopic studies.
  • Engineering hydrophobic mutations in the disordered DNA-binding domain of CytR.

Main Results:

  • Synergistic hydrophobic mutations promoted structure, compactness, and stability in the CytR DNA-binding domain.
  • The double mutant exhibited properties of a fully ordered domain with weak cooperativity.
  • Mutant binding affinity to cognate DNA was marginally higher, with notable differences in noncognate DNA binding.

Conclusions:

  • Non-additive hydrophobic effects play a dominant role in the evolution of order in disordered proteins.
  • These findings have implications for protein design and functional manipulation, potentially extending to folded proteins.
  • Hydrophobic substitutions can lead to emergent structural order and altered function in intrinsically disordered proteins.