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 Experiment Videos

Exploring the sequence-structure-function relationship for the intrinsically disordered βγ-crystallin Hahellin.

Meng Gao1, Fei Yang1, Lei Zhang1

  • 1a Department of Biological Engineering and Institute of Biomedical and Pharmaceutical Sciences , Hubei University of Technology , Wuhan , Hubei 430068 , China.

Journal of Biomolecular Structure & Dynamics
|April 11, 2017
PubMed
Summary
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

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

Sort by
Same author

Rapamycin alleviates inflammation and muscle weakness, while altering the Treg/Th17 balance in a rat model of myasthenia gravis.

Bioscience reports·2017
Same author

Stroma-derived Fibrinogen-like Protein 2 Activates Cancer-associated Fibroblasts to Promote Tumor Growth in Lung Cancer.

International journal of biological sciences·2017
Same author

Cross-resistance to purified Bt proteins, Bt corn and Bt cotton in a Cry2Ab2-corn resistant strain of Spodoptera frugiperda.

Pest management science·2017
Same author

Abnormal asymmetry in benign epilepsy with unilateral and bilateral centrotemporal spikes: A combined fMRI and DTI study.

Epilepsy research·2017
Same author

Lkb1 maintains T<sub>reg</sub> cell lineage identity.

Nature communications·2017
Same author

Corrigendum: EpCAM-dependent extracellular vesicles from intestinal epithelial cells maintain intestinal tract immune balance.

Nature communications·2017

βγ-Crystallins are proteins that can be intrinsically disordered. This study reveals sequence factors promoting disorder in Hahellin, a βγ-crystallin, offering insights into protein structure-function relationships.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Protein Science

Background:

  • βγ-Crystallins are protein superfamilies characterized by Greek key motifs.
  • Some βγ-crystallin domains bind calcium ions (Ca2+) and exhibit conformational changes.
  • Hahellin, a βγ-crystallin from Hahella chejuensis, is intrinsically disordered and folds upon Ca2+ binding.

Purpose of the Study:

  • To investigate the sequence-structure relationship governing conformational disorder in the βγ-crystallin superfamily.
  • To identify factors contributing to the disordered state of apo-Hahellin.
  • To analyze disorder propensities in other putative disordered βγ-crystallin domains.

Main Methods:

  • Comparative sequence and structure analysis of Hahellin and Protein S.
Keywords:
crystallindisorder analysisenergy frustrationintrinsically disordered proteinssequence–structure relationship

Related Experiment Videos

  • Computational biophysical techniques were employed.
  • Analysis of disorder propensities in related βγ-crystallin domains.

    • Main Results:

    • Several factors promote apo-Hahellin's disordered state: a C-terminal disorder-prone region, high energetic frustrations, and low contact density.
    • The study identified specific sequence features linked to conformational disorder in βγ-crystallins.
    • Disorder propensities were analyzed for other potential disordered βγ-crystallin domains.

    Conclusions:

    • The findings provide crucial insights into the sequence-structure-function relationships within the βγ-crystallin superfamily.
    • Understanding these relationships can aid in predicting and designing proteins with specific conformational properties.
    • This research contributes to the broader understanding of intrinsically disordered proteins and their regulation.