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

Cytoskeletal Proteins in Bacteria01:29

Cytoskeletal Proteins in Bacteria

4.3K
Bacterial cells were initially considered simple, randomly organized structures lacking a cytoskeleton. However, the discovery of cytoskeleton homologs in bacteria led to the change of this opinion. Bacterial cytoskeletal filaments regulate the cell shape, cell polarity, cell division, and partitioning of plasmids during cell division. It was later discovered that bacterial cytoskeletal proteins, mainly actin and tubulin homologs, are diverse compared to their eukaryotic counterparts. On the...
4.3K
Factors Affecting Protein-Drug Binding: Protein-Related Factors01:20

Factors Affecting Protein-Drug Binding: Protein-Related Factors

576
Drug binding to proteins is a key aspect of pharmacokinetics and can influence a drug's distribution, absorption, and elimination in the body. Several factors, including the drug's physiochemical properties, protein concentration, disease states, and the number of binding sites on the protein, influence this process.
The physicochemical properties of a drug play a significant role in its ability to bind to proteins. Lipophilic drugs, which dissolve in fats, oils, and lipids, can be...
576
The Equilibrium Binding Constant and Binding Strength02:18

The Equilibrium Binding Constant and Binding Strength

15.2K
The equilibrium binding constant (Kb) quantifies the strength of a protein-ligand interaction. Kb can be calculated as follows when the reaction is at equilibrium:
15.2K
Drug Distribution: Plasma Protein Binding01:29

Drug Distribution: Plasma Protein Binding

9.0K
Drugs predominantly attach to plasma proteins, with only a small percentage remaining unbound. The unbound portion can be calculated as one minus the bound fraction. Acidic drugs form large, inactive complexes by reversibly binding to plasma albumin, which prevents them from diffusing across biological barriers. These drug-protein complexes act as reservoirs for the drugs. As the concentration of unbound drugs decreases, these complexes quickly dissociate to release the free drug, maintaining...
9.0K
Protein-Drug Binding: Determination Methods01:22

Protein-Drug Binding: Determination Methods

676
Determining protein-drug binding can be achieved through indirect and direct methods, each providing valuable insights into the interaction between proteins and drugs.
Indirect methods involve isolating the bound drug from its free form in biological samples such as blood, serum, or plasma. These techniques aim to measure the percentage of drugs bound to proteins. Equilibrium dialysis is a commonly used method where the free drug concentration at equilibrium is measured by separating the bound...
676
Single-Strand DNA Binding Proteins01:03

Single-Strand DNA Binding Proteins

16.8K
For successful DNA replication, the unwinding of double-stranded DNA must be accompanied by stabilization and protection of the separated single strands of the DNA. This crucial task is performed by single-strand DNA-binding (SSB) proteins. They bind to the DNA in a sequence-independent manner, which means that the nitrogenous bases of the DNA need not be present in a specific order for binding of SSB proteins to it. The binding of SSB proteins straightens single-stranded DNA (ssDNA) and makes...
16.8K

You might also read

Related Articles

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

Sort by
Same author

Essential role of choline for pneumococcal virulence in an experimental model of meningitis.

Journal of internal medicine·2008
Same author

Role of PBP1 in cell division of Staphylococcus aureus.

Journal of bacteriology·2007
Same author

Role of VraSR in antibiotic resistance and antibiotic-induced stress response in Staphylococcus aureus.

Antimicrobial agents and chemotherapy·2006
Same author

Role of murF in cell wall biosynthesis: isolation and characterization of a murF conditional mutant of Staphylococcus aureus.

Journal of bacteriology·2006
Same author

Role of murE in the Expression of beta-lactam antibiotic resistance in Staphylococcus aureus.

Journal of bacteriology·2004
Same author

Alterations of cell wall structure and metabolism accompany reduced susceptibility to vancomycin in an isogenic series of clinical isolates of Staphylococcus aureus.

Journal of bacteriology·2003

Related Experiment Video

Updated: Feb 11, 2026

FLIM-FRET Measurements of Protein-Protein Interactions in Live Bacteria.
09:26

FLIM-FRET Measurements of Protein-Protein Interactions in Live Bacteria.

Published on: August 25, 2020

10.0K

Penicillin-binding proteins in bacteria

A Tomasz

    Annals of Internal Medicine
    |April 1, 1982
    PubMed
    Summary
    This summary is machine-generated.

    Renewed interest in beta-lactam antibiotics surged due to sodium dodecyl sulphate electrophoresis. This technique identified penicillin binding proteins, revealing new insights into how these antibiotics target bacteria.

    More Related Videos

    An Assay for Quantifying Protein-RNA Binding in Bacteria
    07:02

    An Assay for Quantifying Protein-RNA Binding in Bacteria

    Published on: June 12, 2019

    7.0K
    Pull-down of Calmodulin-binding Proteins
    07:51

    Pull-down of Calmodulin-binding Proteins

    Published on: January 23, 2012

    25.9K

    Related Experiment Videos

    Last Updated: Feb 11, 2026

    FLIM-FRET Measurements of Protein-Protein Interactions in Live Bacteria.
    09:26

    FLIM-FRET Measurements of Protein-Protein Interactions in Live Bacteria.

    Published on: August 25, 2020

    10.0K
    An Assay for Quantifying Protein-RNA Binding in Bacteria
    07:02

    An Assay for Quantifying Protein-RNA Binding in Bacteria

    Published on: June 12, 2019

    7.0K
    Pull-down of Calmodulin-binding Proteins
    07:51

    Pull-down of Calmodulin-binding Proteins

    Published on: January 23, 2012

    25.9K

    Area of Science:

    • Microbiology
    • Biochemistry
    • Pharmacology

    Background:

    • Beta-lactam antibiotics are crucial antibacterial agents.
    • Recent years show increased research interest in beta-lactams.
    • Understanding their precise mechanism of action remains vital.

    Purpose of the Study:

    • To explore the renewed interest in beta-lactam antibiotics.
    • To highlight the role of sodium dodecyl sulphate electrophoresis in this field.
    • To discuss how new techniques have advanced our understanding of beta-lactam action.

    Main Methods:

    • Sodium dodecyl sulphate electrophoresis was employed.
    • Identification of bacterial membrane components, specifically penicillin binding proteins.
    • Use of radioactive penicillin to detect target binding.

    Main Results:

    • The technique facilitated identification of penicillin binding proteins.
    • These proteins are likely primary targets of penicillin action.
    • Novel observations have significantly updated the understanding of beta-lactam mechanisms.

    Conclusions:

    • Sodium dodecyl sulphate electrophoresis is a powerful tool for studying beta-lactam antibiotics.
    • Penicillin binding proteins are key targets, and their study has advanced the field.
    • Our view of beta-lactam antibiotic action has been substantially modified by recent research.