Related Experiment Video

Updated: Mar 9, 2026

Production, Crystallization and Structure Determination of C. difficile PPEP-1 via Microseeding and Zinc-SAD
13:34

Production, Crystallization and Structure Determination of C. difficile PPEP-1 via Microseeding and Zinc-SAD

Published on: December 30, 2016

12.0K

Impact of macromolecular crowding on structure and properties of pepsin and trypsin

Wala Gtari1, Houda Bey1, Adel Aschi1

  • 1Université de Tunis El Manar, Faculté des Sciences de Tunis, LR99ES16 Laboratoire Physique de la Matière Molle et de la Modélisation Électromagnétique, 2092 Tunis, Tunisia.

Materials Science & Engineering. C, Materials for Biological Applications
|December 28, 2016
PubMed

Keywords:
Aging effectChemical denaturationDynamic light scatteringExcluded volume effectMacromolecular crowdingSmall angles static light scattering

More Related Videos

Optimizing the Growth of Endothiapepsin Crystals for Serial Crystallography Experiments09:52

Optimizing the Growth of Endothiapepsin Crystals for Serial Crystallography Experiments

Published on: February 4, 2021

2.8K
The Importance of Correct Protein Concentration for Kinetics and Affinity Determination in Structure-function Analysis19:16

The Importance of Correct Protein Concentration for Kinetics and Affinity Determination in Structure-function Analysis

Published on: March 17, 2010

21.2K

Related Concept Videos

Protein Organization01:24

Protein Organization

Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence....
9.9K
Protein Folding01:22

Protein Folding

Overview
129.6K
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...
12.0K
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...
20.6K