Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Search research articles

Related Experiment Videos

Membrane proteins: shaping up.

Chen-Ni Chin¹, Gunnar von Heijne, Jan-Willem L de Gier

¹Department Molecular Biophysics and Biochemistry, Yale University, Bass 429, 266 Whitney Avenue, New Haven, CT 06520, USA.

Trends in Biochemical Sciences

|June 22, 2002

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

Calmodulin assists during co-translational folding of the K<sub>V</sub>7.2 channel calcium responsive domain.

Protein science : a publication of the Protein Society·2026

Same author

Cotranslational Folding and "Constrained Monomers" in the Maturation of HIV-1 Protease.

Journal of molecular biology·2026

Same author

Quasi-continuous cotranslational compaction and folding of a multidomain protein.

bioRxiv : the preprint server for biology·2026

Same author

Development of a potent monoclonal antibody for treatment of human metapneumovirus infections.

Nature communications·2026

Same author

SARS-CoV-2 membrane protein biogenesis.

bioRxiv : the preprint server for biology·2026

Same author

Cotranslational folding and maturation of HIV-1 protease.

bioRxiv : the preprint server for biology·2025

Same journal

Peptideins: Navigating the gray zone of the proteome.

Trends in biochemical sciences·2026

Same journal

A metabolon channels nicotine biosynthesis.

Trends in biochemical sciences·2026

Same journal

Better call chaperone.

Trends in biochemical sciences·2026

Same journal

Biochemistry at scale: Seeing both the forest and the trees.

Trends in biochemical sciences·2026

Same journal

Voices across Asia and Oceania: Biochemistry across borders.

Trends in biochemical sciences·2026

Same journal

Metabolic control of RNA splicing by polyamines.

Trends in biochemical sciences·2026

See all related articles

Understanding integral membrane protein folding in vivo remains a challenge. Research is exploring how translocon-mediated assembly, not just lipid interactions, constrains final protein structures.

Area of Science:

Biochemistry
Molecular Biology
Structural Biology

Background:

Significant advancements in identifying factors for integral membrane protein biosynthesis.
Growing understanding of membrane protein structure and helix-helix interaction stability in lipid environments.

Purpose of the Study:

To elucidate the in vivo folding mechanisms of integral membrane proteins.
To investigate the constraints imposed by translocon-mediated assembly on protein structure.

Main Methods:

Characterization of biosynthesis factors.
Analysis of membrane protein structure and stability.
Investigating translocon-mediated assembly processes.

Main Results:

Related Experiment Videos

Progress in identifying key biosynthesis factors for helix-bundle proteins.

Expanded knowledge on forces stabilizing protein structures within lipid bilayers.

Conclusions:

The precise in vivo folding pathway of membrane proteins is not fully understood.
Translocon-mediated assembly introduces specific constraints on final protein structures beyond thermodynamic lipid interactions.