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Related Concept Videos

Next-generation Sequencing03:00

Next-generation Sequencing

The first human genome sequencing project cost $2.7 billion and was declared complete in 2003, after 15 years of international cooperation and collaboration between several research teams and funding agencies. Today, with the advent of next-generation sequencing technologies, the cost and time of sequencing a human genome have dropped over 100 fold.
Next-Generation Sequencing Methods
Although all next-generation methods use different technologies, they all share a set of standard features.
Southern Blot02:57

Southern Blot

Agarose gel electrophoresis is very useful in separating DNA fragments by size. Running a DNA ladder containing fragments of the known length alongside the sample helps determine the approximate length of the sample DNA fragments. However, additional steps are needed to verify the sequence identity of the sample DNA fragments.
Denatured DNA fragments must be transferred onto a carrier membrane from the gel to make it accessible to a probe - a small ssDNA fragment complementary to the target DNA...
Proofreading01:31

Proofreading

Synthesis of new DNA molecules is carried out by the enzyme DNA polymerase, which adds nucleotides on the daughter strand complementary to the template DNA strand. DNA polymerase has a higher affinity to add the correct base and ensures fidelity during DNA replication. Furthermore,  it exhibits proofreading activity during replication, using an exonuclease domain that cuts off incorrect nucleotides from the nascent DNA strand.
Errors During Replication are Corrected by the DNA Polymerase Enzyme

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Related Experiment Video

Updated: May 31, 2026

Residue-Specific Exchange of Proline by Proline Analogs in Fluorescent Proteins: How "Molecular Surgery" of the Backbone Affects Folding and Stability
10:31

Residue-Specific Exchange of Proline by Proline Analogs in Fluorescent Proteins: How "Molecular Surgery" of the Backbone Affects Folding and Stability

Published on: February 3, 2022

An advance in proline ligation.

Shiying Shang1, Zhongping Tan, Suwei Dong

  • 1Laboratory for Bioorganic Chemistry, Sloan-Kettering Institute for Cancer Research, 1275 York Avenue, New York, New York 10065, USA.

Journal of the American Chemical Society
|June 24, 2011
PubMed
Summary
This summary is machine-generated.

Native chemical ligation (NCL) enables laboratory protein synthesis. A new method combining NCL and metal-free deprotection (MFD) now allows ligation at N-terminal proteins, overcoming previous limitations with proline thioesters.

Related Experiment Videos

Last Updated: May 31, 2026

Residue-Specific Exchange of Proline by Proline Analogs in Fluorescent Proteins: How "Molecular Surgery" of the Backbone Affects Folding and Stability
10:31

Residue-Specific Exchange of Proline by Proline Analogs in Fluorescent Proteins: How "Molecular Surgery" of the Backbone Affects Folding and Stability

Published on: February 3, 2022

Area of Science:

  • Biochemistry
  • Chemical Biology
  • Synthetic Biology

Background:

  • Native chemical ligation (NCL) is a powerful technique for peptide and protein synthesis.
  • Ligation at C-terminal proline residues remains challenging due to the poor reactivity of proline thioesters.

Purpose of the Study:

  • To develop a novel strategy for efficient protein ligation at N-terminal proline sites.
  • To overcome the limitations of traditional NCL methods when dealing with proline residues.

Main Methods:

  • The study combined Native Chemical Ligation (NCL) with metal-free deprotection (MFD).
  • This approach was specifically designed to address the reactivity issues associated with proline thioesters.

Main Results:

  • Demonstrated the feasibility of ligation at an N-terminal protein site.
  • Successfully achieved ligation despite the inherent challenges of proline thioester reactivity.

Conclusions:

  • The combined NCL and MFD strategy provides a viable method for protein synthesis involving N-terminal proline.
  • This advancement expands the utility of NCL for constructing complex protein molecules.