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

Conformational and sequence signatures in beta helix proteins.

Prathima Iengar1, N V Joshi, Padmanabhan Balaram

  • 1Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560012, India.

Structure (London, England : 1993)
|March 15, 2006
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

Insights into the role of internal catalysts in asparagine-to-succinimide conversion in a hyperthermophilic glutamine amidotransferase.

The Journal of biological chemistry·2026
Same author

Using the Reactome Graph Database to generate pathway fingerprints for cancer-related genes, and using the fingerprints to gain insights into cancer, comorbidity, and cancer gene networks.

Computational biology and chemistry·2025
Same author

Side Chain Driven Mass Spectral Fragmentation of Lys Containing Peptides: C<sup>α</sup>-CO Bond Cleavage in Xxx-Lys-Xxx Sequences.

Journal of the American Society for Mass Spectrometry·2025
Same author

Resurrection of the Helical Hairpin Hypothesis for Understanding Coronavirus Fusion.

The Journal of membrane biology·2025
Same author

Sequence of the SARS-CoV-2 Spike Transmembrane Domain Encodes Conformational Dynamics.

The journal of physical chemistry. B·2024
Same author

Albumin Oxidation and Albumin Glycation Discordance During Type 2 Diabetes Therapy: Biological and Clinical Implications.

Metabolic syndrome and related disorders·2024

Beta helix proteins fold via specific conformational rules. Researchers analyzed left- and right-handed structures, revealing distinct patterns in coil formation and residue preferences essential for protein folding.

Area of Science:

  • Structural biology
  • Protein folding
  • Biophysics

Background:

  • Beta helix proteins possess a repetitive fold comprising beta-helical coils.
  • These coils are formed by three strand segments and three loop segments.
  • Understanding their folding rules is crucial for protein structure prediction.

Purpose of the Study:

  • To investigate conformational features at equivalent positions in successive coils of beta helix proteins.
  • To elucidate the conformational rules governing the folding of left- and right-handed beta helices.
  • To explore backbone conformational parameters enabling loopless beta helices (Perutz nanotubes).

Main Methods:

  • Analysis of a dataset of left- and right-handed beta helix proteins.
  • Examination of conformational sequences at specific positions within coils.

Related Experiment Videos

  • Investigation of backbone dihedral angles (phi, psi).

    • Main Results:

    • Left-handed beta helices utilize a P(II)-P(II)-alpha(L)-P(II) corner conformation, imposing sequence restrictions (e.g., G and small uncharged residues).
    • Right-handed beta helices exhibit conserved loop conformations (4-6 residues) and an alpha-helical residue at the C-terminus of L2 loops.
    • Identified backbone conformational parameters that allow for the formation of continuous, loopless beta helices.

    Conclusions:

    • Specific conformational rules dictate the folding of beta helix proteins.
    • Left- and right-handed beta helices employ distinct strategies for achieving their structures.
    • Insights gained can inform the design of novel protein structures and Perutz nanotubes.