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

Peptide Identification Using Tandem Mass Spectrometry01:33

Peptide Identification Using Tandem Mass Spectrometry

Tandem mass spectrometry, also known as MS/MS or MS2, is an analytical technique that employs two mass analyzers. Essentially it is a series of mass spectrometers that helps isolate a particular biomolecule and then helps study its chemical properties.
This technique helps gather information regarding the protein from which the peptide was obtained and to study the peptides’ amino acid sequence. Identifying peptides from a complex mixture is an important component of the growing field of...

You might also read

Related Articles

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

Sort by
Same author

Self-supported catalysts.

Chemical reviews·2008
Same author

Preparation of honeycomb scaffold with hierarchical porous structures by core-crosslinked core-corona nanoparticles.

Journal of colloid and interface science·2008
Same author

[The local control of radiotherapy following Ivor-Lewis esophagectomy in the patients with stage II A middle-third thoracic esophageal cancer].

Zhonghua wai ke za zhi [Chinese journal of surgery]·2008
Same author

Magnetic loading of carbon nanotube/nano-Fe(3)O(4) composite for electrochemical sensing.

Talanta·2008
Same author

Carbon nanotube/polystyrene composite electrode for microchip electrophoretic determination of rutin and quercetin in Flos Sophorae Immaturus.

Talanta·2008
Same author

[Observation on efficacy of large volume whole lung lavage in treatment of pneumoconiosis].

Zhonghua lao dong wei sheng zhi ye bing za zhi = Zhonghua laodong weisheng zhiyebing zazhi = Chinese journal of industrial hygiene and occupational diseases·2008

Related Experiment Video

Updated: Jun 28, 2026

Optimal Preparation of Formalin Fixed Samples for Peptide Based Matrix Assisted Laser Desorption/Ionization Mass Spectrometry Imaging Workflows
08:16

Optimal Preparation of Formalin Fixed Samples for Peptide Based Matrix Assisted Laser Desorption/Ionization Mass Spectrometry Imaging Workflows

Published on: January 16, 2018

Efficient chymotryptic proteolysis enhanced by infrared radiation for peptide mapping.

Sheng Wang1, Ting Liu, Luyan Zhang

  • 1School of Pharmacy and Department of Chemistry, Fudan University, Shanghai 200032, China.

Journal of Proteome Research
|October 22, 2008
PubMed
Summary

Infrared (IR) radiation significantly speeds up chymotryptic proteolysis for peptide mapping. This novel IR-assisted method reduces digestion time to 5 minutes, enabling efficient protein identification.

More Related Videos

Detection of Protease Activity by Fluorescent Peptide Zymography
09:56

Detection of Protease Activity by Fluorescent Peptide Zymography

Published on: January 20, 2019

Related Experiment Videos

Last Updated: Jun 28, 2026

Optimal Preparation of Formalin Fixed Samples for Peptide Based Matrix Assisted Laser Desorption/Ionization Mass Spectrometry Imaging Workflows
08:16

Optimal Preparation of Formalin Fixed Samples for Peptide Based Matrix Assisted Laser Desorption/Ionization Mass Spectrometry Imaging Workflows

Published on: January 16, 2018

Detection of Protease Activity by Fluorescent Peptide Zymography
09:56

Detection of Protease Activity by Fluorescent Peptide Zymography

Published on: January 20, 2019

Area of Science:

  • Biochemistry
  • Analytical Chemistry
  • Proteomics

Background:

  • Chymotryptic proteolysis is crucial for peptide mapping.
  • Conventional methods can be time-consuming.
  • Enhancing proteolysis efficiency is vital for high-throughput analysis.

Purpose of the Study:

  • To investigate the use of infrared (IR) radiation to enhance chymotryptic proteolysis.
  • To evaluate the efficiency and performance of IR-assisted digestion for peptide mapping.
  • To demonstrate a faster and simpler proteolysis strategy.

Main Methods:

  • Protein solutions with chymotrypsin were digested under an IR lamp at 37°C.
  • Bovine serum albumin (BSA) and cytochrome c (Cyt-c) were used to test the method.
  • Complex protein samples, including human serum, were also analyzed.

Main Results:

  • IR-assisted chymotryptic proteolysis significantly reduced digestion time to 5 minutes.
  • Peptide mapping achieved comparable sequence coverages to conventional methods.
  • The approach proved effective for complex protein mixtures like human serum.

Conclusions:

  • IR-assisted chymotryptic proteolysis is a simple, efficient, and rapid technique.
  • This method offers a promising strategy for high-throughput protein identification.
  • The reduced digestion time enhances the overall workflow for proteomic analysis.