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 Bonds02:43

Peptide Bonds

74.0K
A peptide bond covalently attaches amino acids through a dehydration reaction. One amino acid's carboxyl group and another amino acid's amino group combine, releasing a water molecule. The resulting bond is the peptide bond. The products that such linkages form are peptides. As more amino acids join this growing chain, the resulting chain is a polypeptide. Each polypeptide has a free amino group at one end. This end has the N-terminal, or the amino-terminal, and the other end has a free...
74.0K
¹³C NMR: Distortionless Enhancement by Polarization Transfer (DEPT)01:20

¹³C NMR: Distortionless Enhancement by Polarization Transfer (DEPT)

1.0K
When proton-coupled carbon-13 spectra are simplified by a broadband proton decoupling technique, structural information about the coupled protons is lost. Distortionless enhancement by polarization transfer (DEPT) is a technique that provides information on the number of hydrogens attached to each carbon in a molecule. While the DEPT experiment utilizes complex pulse sequences, the pulse delay and flip angle are specifically manipulated. The resulting signals have different phases depending on...
1.0K
Protein Folding01:25

Protein Folding

7.9K
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...
7.9K
Amino acids03:42

Amino acids

88.6K
Amino acids are the monomers that comprise proteins. Each amino acid has the same fundamental structure, which consists of a central carbon atom, or the alpha (α) carbon, bonded to an amino group (NH2), a carboxyl group (COOH), and to a hydrogen atom. Every amino acid also has another atom or group of atoms bonded to the central atom known as the R group. There are 20 common amino acids present in proteins, each with a different R group. Variation in the amino acid sequence is responsible...
88.6K

You might also read

Related Articles

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

Sort by
Same author

Mussel-Inspired Copolyether Brushes: Synergistic Catechol-Amine Interactions for Enhanced Adhesion and Antifouling Performance.

Biomacromolecules·2026
Same author

Stimuli-Responsive Zirconium-Based Metal-Organic Frameworks for Targeted Cancer Drug Delivery.

ACS applied materials & interfaces·2026
Same author

Biomimetic peptide self-assembly: interfacing with biomacromolecules to regulate cellular signaling.

Experimental & molecular medicine·2026
Same author

Self-Assembled Nanomaterials for ER-Targeted Cancer Therapy: From Molecular Design to Therapeutic Applications.

Biomacromolecules·2026
Same author

Bst2-targeted senotherapy restores visual function by eliminating senescent retinal cells.

Nature communications·2026
Same author

A strippable catechol-terminated polyurethane coating for large-area radioactive cesium decontamination.

Materials horizons·2026
Same journal

Active learning-driven global search for neutral gold clusters <i>via</i> neural network potential.

Physical chemistry chemical physics : PCCP·2026
Same journal

Development of indole-based hydration-sensitive fluorescent nucleoside analogues: experimental and computational studies.

Physical chemistry chemical physics : PCCP·2026
Same journal

Gradient engineering enabled thermoelectric performance optimization in LaP/LaAs heterostructures.

Physical chemistry chemical physics : PCCP·2026
Same journal

Barrierless proton and hydrogen atom migrations in photoionized benzaldehyde clusters result in benzyl alcohol formation: an ion-molecule perspective.

Physical chemistry chemical physics : PCCP·2026
Same journal

Weakly protonated polyethylenimine induces SiC flocculation in alkaline suspensions.

Physical chemistry chemical physics : PCCP·2026
Same journal

Accurate interdomain contacts in a mixed folded protein from NMR-guided coarse-grained simulations.

Physical chemistry chemical physics : PCCP·2026
See all related articles

Related Experiment Video

Updated: Jun 19, 2025

Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry
11:37

Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry

Published on: November 29, 2013

18.5K

Specific interaction between the DSPHTELP peptide and various functional groups.

Haeun Kwon1, Seongeon Jin2, Jina Ko1

  • 1School of Energy and Chemical Engineering, Ulsan National Institute of Science and Technology (UNIST), 50 UNIST-gil, Ulsan 44919, Republic of Korea. dongwoog.lee@unist.ac.kr.

Physical Chemistry Chemical Physics : PCCP
|July 24, 2024
PubMed
Summary
This summary is machine-generated.

M13 bacteriophage peptides can be engineered for nanobiotechnology. This study quantifies the DSPHTELP peptide

More Related Videos

Wet Chemistry and Peptide Immobilization on Polytetrafluoroethylene for Improved Cell-adhesion
06:15

Wet Chemistry and Peptide Immobilization on Polytetrafluoroethylene for Improved Cell-adhesion

Published on: August 15, 2016

7.7K
A Hydrogen-Deuterium Exchange Mass Spectrometry HDX-MS Platform for Investigating Peptide Biosynthetic Enzymes
11:32

A Hydrogen-Deuterium Exchange Mass Spectrometry HDX-MS Platform for Investigating Peptide Biosynthetic Enzymes

Published on: May 4, 2020

8.0K

Related Experiment Videos

Last Updated: Jun 19, 2025

Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry
11:37

Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry

Published on: November 29, 2013

18.5K
Wet Chemistry and Peptide Immobilization on Polytetrafluoroethylene for Improved Cell-adhesion
06:15

Wet Chemistry and Peptide Immobilization on Polytetrafluoroethylene for Improved Cell-adhesion

Published on: August 15, 2016

7.7K
A Hydrogen-Deuterium Exchange Mass Spectrometry HDX-MS Platform for Investigating Peptide Biosynthetic Enzymes
11:32

A Hydrogen-Deuterium Exchange Mass Spectrometry HDX-MS Platform for Investigating Peptide Biosynthetic Enzymes

Published on: May 4, 2020

8.0K

Area of Science:

  • Nanobiotechnology
  • Materials Science
  • Biochemistry

Background:

  • M13 bacteriophages offer a versatile platform for nanobiotechnology due to their unique properties.
  • Genetic engineering of M13 bacteriophage coat proteins (pVIII) allows for tailored functionalization.
  • Engineered M13 bacteriophages, like DSPH, exhibit specific adhesion to single-walled carbon nanotubes (SWCNTs).

Purpose of the Study:

  • To synthesize the DSPHTELP peptide and analyze its interaction forces with different functional groups.
  • To elucidate the predominant molecular interaction mechanisms between the DSPHTELP peptide and surfaces.
  • To provide quantitative and qualitative understanding of the DSPHTELP peptide's interaction with SWCNTs.

Main Methods:

  • Peptide synthesis of the 8-mer DSPHTELP sequence.
  • Surface Forces Apparatus (SFA) measurements to quantify interaction forces.
  • Analysis of peptide-surface interactions across varying pH levels.

Main Results:

  • The DSPHTELP 8-mer peptide exhibits strongest binding to methyl (CH3) groups.
  • Hydrophobic interactions were identified as the predominant binding mechanism.
  • Quantitative data (Wad = 13.74 ± 1.04 mJ m-2 at pH 3.0) supports the role of hydrophobic forces.

Conclusions:

  • Hydrophobic interactions are the primary driver for DSPHTELP peptide adhesion.
  • This understanding clarifies the molecular basis for DSPH M13 bacteriophage interaction with SWCNTs.
  • The findings support the use of engineered M13 bacteriophages in developing advanced hybrid materials.