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

Sequence space, folding and protein design

M H Cordes1, A R Davidson, R T Sauer

  • 1Department of Biology, Massachusetts Institute of Technology, Cambridge 02139, USA.

Current Opinion in Structural Biology
|February 1, 1996
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

Pyelo-Nephritis Consequent upon the Presence of Calculi and Over-distention of the Bladder for Three Weeks-Twenty-one Calculi Found in the Bladder.

Buffalo medical and surgical journal·2023
Same author

Arsenical Poisoning-The "Kloss Case"-Unusual Post-mortem Appearances.

Buffalo medical and surgical journal·2023
Same author

"Sewer Gas and Its Dangers," Letter from Prof. F. H. Hamilton.

Buffalo medical and surgical journal·2023
Same author

"Sewer Gas" and Its Dangers.

Buffalo medical and surgical journal·2023
Same author

Diseases of the Scalp.-The Syphilides: A Clinical Lecture Delivered at the Hospital of the Sisters of Charity.

Buffalo medical and surgical journal·2023
Same author

Hæmaturia as a Symptom of Diseases of the Genito-Urinary Organs.

Buffalo medical and surgical journal·2023
Same journal

Tomogram exploration through template matching and deep learning.

Current opinion in structural biology·2026
Same journal

A comparative review of cryo-electron ptychography: Biological applications and future perspectives.

Current opinion in structural biology·2026
Same journal

Metabolic disruptions through a three-dimensional genomic lens.

Current opinion in structural biology·2026
Same journal

Collective variable design for biomolecular conformational dynamics.

Current opinion in structural biology·2026
Same journal

Polymer scaling in protein crowding: From dilute coils to semidilute meshes.

Current opinion in structural biology·2026
Same journal

Tuning the physicochemical properties of rationally designed protein-based biomolecular condensates.

Current opinion in structural biology·2026
See all related articles

Protein design advances create molecules mimicking natural proteins. Key factors for protein folding and stability include hydrophobic residue placement and core packing, alongside other structural elements.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Protein Engineering

Background:

  • Current protein design strategies aim to create novel molecules with natural protein-like properties.
  • Understanding the sequence-structure-function relationship is crucial for successful protein design.
  • Existing knowledge highlights the importance of specific amino acid residues and their arrangement in protein folding and stability.

Purpose of the Study:

  • To elucidate the critical sequence determinants governing protein folding and stability.
  • To identify key design principles for creating functional de novo proteins.
  • To contribute to the broader understanding of protein structure-stability relationships.

Main Methods:

  • Computational protein design simulations.

Related Experiment Videos

  • Analysis of sequence-structure relationships in natural and designed proteins.
  • Experimental validation of designed protein properties (implied).

    • Main Results:

    • Successful protein design yields molecules with properties comparable to natural proteins.
    • Hydrophobic residue placement and the formation of a well-packed hydrophobic core are paramount for protein stability.
    • Buried polar interactions, turn motifs, capping, and secondary structure propensities play a secondary role in stability.

    Conclusions:

    • Protein design is advancing, producing molecules with natural protein characteristics.
    • Optimizing hydrophobic interactions and core packing is essential for achieving stable designed proteins.
    • Further research can refine design principles by considering the interplay of various structural factors.