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

Reading protein sequences backwards

E Lacroix1, A R Viguera, L Serrano

  • 1Biostructure and Biocomputing Department, European Molecular Biology Laboratory, Heidelberg, Germany.

Folding & Design
|May 5, 1998
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

Nefopam Misuse: A Cross-Sectional Study in France.

European journal of pain (London, England)·2025
Same author

Preliminary steps for fabrication of microfluidic systems for swine sperm sorting: Materials, perfusing systems and flow.

Research in veterinary science·2024
Same author

Assessment of seasonal and annual patterns in phosphorus content in a monitored catchment through a partitioning approach based on hydrometeorological data.

Environmental research·2023
Same author

Impact of outdoor air pollution on severity and mortality in COVID-19 pneumonia.

The Science of the total environment·2023
Same author

Three-year efficacy of switching to dolutegravir plus lamivudine: A real-world study.

HIV medicine·2023
Same author

Real-life analysis on safety and efficacy of asciminib for ponatinib pretreated patients with chronic myeloid leukemia.

Annals of hematology·2022
Same journal

Fishing for folding nuclei in lattice models and proteins.

Folding & design·1999
Same journal

Folding nucleus: specific or multiple? Insights from lattice models and experiments.

Folding & design·1999
Same journal

Sequential domain refolding of pig muscle 3-phosphoglycerate kinase: kinetic analysis of reactivation.

Folding & design·1999
Same journal

Discrete molecular dynamics studies of the folding of a protein-like model.

Folding & design·1999
Same journal

Knowledge-based structure prediction of MHC class I bound peptides: a study of 23 complexes.

Folding & design·1999
Same journal

How and why phosphotyrosine-containing peptides bind to the SH2 and PTB domains.

Folding & design·1999
See all related articles

Retro proteins, sequences read backward, do not fold into functional structures. Experimental and computational analyses confirm these proteins remain unfolded, unlike their parent sequences.

Area of Science:

  • Protein folding and biophysics
  • Structural biology
  • Computational biology

Background:

  • Reading a protein sequence in reverse yields a new polypeptide with questionable foldability.
  • Previous low-resolution simulations suggested potential native or mirror-image folds for retro proteins.
  • Experimental validation for retro protein folding and structure was lacking.

Purpose of the Study:

  • To investigate the folding potential of retro protein sequences.
  • To computationally model and experimentally test the structure of retro proteins.
  • To determine if retro proteins adopt native or mirror-image folds.

Main Methods:

  • Computational modeling using distance geometry and molecular dynamics for retro sequences.
  • Experimental analysis of retro sequences from alpha-spectrin SH3, Staphylococcal protein A, and Streptococcal protein G.

Related Experiment Videos

  • Assessment of secondary structure propensities in unfolded retro proteins.

    • Main Results:

    • Computational modeling contradicted the possibility of a mirror-image fold for the alpha-spectrin SH3 retro sequence.
    • Experimental evidence showed that retro sequences of SH3, protein A, and protein G are unfolded.
    • Some residual propensities for secondary structure formation were observed in the unfolded retro proteins.

    Conclusions:

    • Retro proteins exhibit no significant structural similarity to their parent sequences, akin to random sequences.
    • Despite shared patterns, retro proteins do not adopt predictable folds.
    • Simple folding models are insufficient for predicting the structure of novel proteins like retro proteins.