Related Experiment Video

Updated: Feb 3, 2026

Interview: Protein Folding and Studies of Neurodegenerative Diseases
19:50

Interview: Protein Folding and Studies of Neurodegenerative Diseases

Published on: July 16, 2008

13.2K

Role of Selenoprotein F in Protein Folding and Secretion: Potential Involvement in Human Disease

Bingyu Ren1,2, Min Liu3,4, Jiazuan Ni5,6

  • 1Shenzhen Key Laboratory of Marine Biotechnology and Ecology, Department of Marine Biology, Shenzhen University, Shenzhen 518060, China. renbingyu89@foxmail.com.

Nutrients
|November 8, 2018
PubMed

Keywords:
endoplasmic reticulum stressprotein folding quality controlseleniumselenoprotein Fsingle nucleotide polymorphismsthiol–disulfide oxidoreductase

More Related Videos

Analysis of Protein Folding, Transport, and Degradation in Living Cells by Radioactive Pulse Chase08:59

Analysis of Protein Folding, Transport, and Degradation in Living Cells by Radioactive Pulse Chase

Published on: February 12, 2019

11.9K
A Convenient and General Expression Platform for the Production of Secreted Proteins from Human Cells07:09

A Convenient and General Expression Platform for the Production of Secreted Proteins from Human Cells

Published on: July 31, 2012

21.9K

Related Concept Videos

Protein Folding01:22

Protein Folding

Overview
127.4K
Protein Folding01:25

Protein Folding

Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
11.5K
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
19.8K
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

15.0K
Role of Proteins in the Human Body01:28

Role of Proteins in the Human Body

Proteins are the building block of life. They are also  the most abundant macromolecules with as many diverse roles in the body. They are part of many structural components that provide unique shapes and structures to animal cells, tissues, and organs. In addition, they also act as biological catalysts and carry out several anabolic and catabolic reactions. Notably, some proteins are chemical messengers and regulate many critical processes, such as metabolism, growth, and development. They...
6.4K
Protein Folding Quality Check in the RER01:29

Protein Folding Quality Check in the RER

ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
5.2K