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 Concept Videos

Bacterial Protein Maturation01:26

Bacterial Protein Maturation

742
Bacterial protein maturation is a tightly regulated process that ensures newly synthesized polypeptides achieve correct functional conformations. This maturation involves a series of modifications, folding events, and quality control steps, often assisted by specialized chaperone proteins.N-Terminal ModificationsThe maturation of bacterial polypeptides begins cotranslationally as the polypeptide exits the ribosome. The first amino acid, N-formylmethionine (fMet), is typically modified at the...
742
Stringent Response in E. coli01:23

Stringent Response in E. coli

519
Bacterial growth is closely tied to nutrient availability, with cells proliferating exponentially under favorable conditions and entering a stationary phase when resources become scarce. This transition is mediated by a regulatory mechanism known as the stringent response, which allows bacteria to adapt to nutrient deprivation by modulating gene expression and metabolic activity.During nutrient scarcity, intracellular amino acid levels decline. It results in the accumulation of uncharged tRNAs...
519

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

In Vivo Incorporation of Photoproteins into GroEL Chaperonin Retaining Major Structural and Functional Properties.

Molecules (Basel, Switzerland)·2023
Same author

Nonspecific Amyloid Aggregation of Chicken Smooth-Muscle Titin: In Vitro Investigations.

International journal of molecular sciences·2023
Same author

Myosin Binding Protein-C Forms Amyloid-Like Aggregates In Vitro.

International journal of molecular sciences·2021
Same author

Bladder reconstruction using autologous smooth muscle cell sheets grafted on a pre-vascularized capsule.

Theranostics·2020
Same author

Tissue expander capsule as an induced vascular bed to prefabricate an axial vascularized buccal mucosa-lined flap for tubularized posterior urethral reconstruction: preliminary results in an animal model.

Asian journal of andrology·2020
Same author

Effect of Single Amino Acid Substitutions by Asn and Gln on Aggregation Properties of Bence-Jones Protein BIF.

International journal of molecular sciences·2019

Related Experiment Video

Updated: Apr 25, 2026

Monitoring the Assembly of a Secreted Bacterial Virulence Factor Using Site-specific Crosslinking
11:33

Monitoring the Assembly of a Secreted Bacterial Virulence Factor Using Site-specific Crosslinking

Published on: December 17, 2013

5.8K

Structural stability of E. coli trigger factor studied by synchrotron small-angle X-ray scattering.

Yi Shi1, Masaji Shinjo2, Jun-Mei Zhou3

  • 1Shanghai Advanced Research Institute, Chinese Academy of Sciences, 99 Haike Road, Zhangjiang Hi-Tech Park, Pudong, Shanghai 201210, China.

Biophysical Chemistry
|August 19, 2014
PubMed
Summary

Small-angle X-ray scattering (SAXS) revealed that the C-terminal region of Escherichia coli trigger factor (TF) is crucial for its structural stability. Truncating this region significantly altered TF

Keywords:
C-terminal truncationFoldingSmall-angle X-ray scatteringStabilityTrigger factor

More Related Videos

Analysis of SEC-SAXS data via EFA deconvolution and Scatter
10:59

Analysis of SEC-SAXS data via EFA deconvolution and Scatter

Published on: January 28, 2021

9.9K
Investigating Receptor-ligand Systems of the Cellulosome with AFM-based Single-molecule Force Spectroscopy
11:34

Investigating Receptor-ligand Systems of the Cellulosome with AFM-based Single-molecule Force Spectroscopy

Published on: December 20, 2013

7.0K

Related Experiment Videos

Last Updated: Apr 25, 2026

Monitoring the Assembly of a Secreted Bacterial Virulence Factor Using Site-specific Crosslinking
11:33

Monitoring the Assembly of a Secreted Bacterial Virulence Factor Using Site-specific Crosslinking

Published on: December 17, 2013

5.8K
Analysis of SEC-SAXS data via EFA deconvolution and Scatter
10:59

Analysis of SEC-SAXS data via EFA deconvolution and Scatter

Published on: January 28, 2021

9.9K
Investigating Receptor-ligand Systems of the Cellulosome with AFM-based Single-molecule Force Spectroscopy
11:34

Investigating Receptor-ligand Systems of the Cellulosome with AFM-based Single-molecule Force Spectroscopy

Published on: December 20, 2013

7.0K

Area of Science:

  • Biophysics
  • Structural Biology
  • Protein Science

Background:

  • Escherichia coli trigger factor (TF) is a crucial molecular chaperone involved in protein folding.
  • Understanding TF's structural dynamics and stability is key to elucidating its chaperone mechanism.

Purpose of the Study:

  • To investigate the structural characteristics and urea-induced unfolding transitions of full-length TF and its mutants.
  • To determine the role of different TF domains in its overall stability and conformation.

Main Methods:

  • Solution small-angle X-ray scattering (SAXS) was employed to analyze protein structure.
  • Radii of gyration (Rg), distance-distribution function (P(r)), and integrated intensity were measured for TF variants.
  • Urea-induced unfolding was monitored to assess protein stability.

Main Results:

  • The C-terminal truncated mutant (TF360) showed significant structural differences and reduced stability compared to full-length TF.
  • The N-domain truncated mutant (MC) maintained a compact structure but exhibited decreased stability.
  • SAXS data provided quantitative measures of compactness and shape changes during unfolding.

Conclusions:

  • The C-terminal region of TF is essential for maintaining its structural integrity and conformational stability.
  • The N-domain contributes to stability but appears relatively independent of the C-terminal region's influence.
  • These findings highlight the domain-specific contributions to TF's function and stability.