Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Molecular Chaperones and Protein Folding

Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...

Protein Folding

Protein Folding

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...

Protein Folding

Protein Folding

Protein Folding Quality Check in the RER

Protein Folding Quality Check in the RER

ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...

Protein Complex Assembly

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types. Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...

The Unfolded Protein Response

The Unfolded Protein Response

The ER is the hub of protein synthesis in a cell. It has robust systems to quality control protein folding and also for degradation of terminally misfolded proteins. Under normal conditions, a small proportion of misfolded proteins that cannot be salvaged need to be transported to the cytoplasm by the ER-associated degradation or ERAD pathways. However, if the ERAD cannot handle the misfolded proteins, the cell activates the unfolded protein response or UPR to adjust the protein folding...

You might also read

Related Articles

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

Sort by

Same author

DNA acidification by citric acid and gallic acid: acid binding site and DNA structural dynamics.

Journal of biomolecular structure & dynamics·2020

Same author

Locating the binding sites of citric acid and gallic acid on milk <i>β</i>-lactoglobulin.

Journal of biomolecular structure & dynamics·2020

Same author

Binding efficacy of aminobenzoic acid derivatives with DNA duplex: drug binding sites and DNA structure and dynamics.

Journal of biomolecular structure & dynamics·2020

Same author

Biomolecular study and conjugation of two para-aminobenzoic acid derivatives with serum proteins: drug binding efficacy and protein structural analysis.

Journal of biomolecular structure & dynamics·2020

Same author

Application and biomolecular study of functionalized folic acid-dendrimer nanoparticles in drug delivery.

Journal of biomolecular structure & dynamics·2020

Same author

Complexation of cis-Pt and trans-Pt(NH<sub>3</sub>)<sub>2</sub>Cl<sub>2</sub> with serum proteins: A potential application for drug delivery.

Journal of biomolecular structure & dynamics·2019

Search research articles

Related Experiment Video

Updated: Jul 9, 2026

Optical Tweezers to Study RNA-Protein Interactions in Translation Regulation

Optical Tweezers to Study RNA-Protein Interactions in Translation Regulation

Published on: February 12, 2022

Protein unfolding in drug-RNase complexes.

J F Neault¹, S Diamantoglou, M Beauregard

¹Department of Chemistry-Biology, University of Québec at Trois-Rivières, Canada G9A 5H7.

Journal of Biomolecular Structure & Dynamics

|December 21, 2007

Summary

This summary is machine-generated.

This study compares how drugs like AZT, cis-Pt, aspirin, and vitamin C affect bovine pancreatic ribonuclease A (RNase A) stability and structure. Spectroscopic analysis reveals significant protein unfolding and conformational changes upon drug binding, impacting RNase A activity.

More Related Videos

Nanomanipulation of Single RNA Molecules by Optical Tweezers

Nanomanipulation of Single RNA Molecules by Optical Tweezers

Published on: August 20, 2014

Probing RNA Structure with Dimethyl Sulfate Mutational Profiling with Sequencing In Vitro and in Cells

Probing RNA Structure with Dimethyl Sulfate Mutational Profiling with Sequencing In Vitro and in Cells

Published on: December 9, 2022

Related Experiment Videos

Last Updated: Jul 9, 2026

Optical Tweezers to Study RNA-Protein Interactions in Translation Regulation

Optical Tweezers to Study RNA-Protein Interactions in Translation Regulation

Published on: February 12, 2022

Nanomanipulation of Single RNA Molecules by Optical Tweezers

Nanomanipulation of Single RNA Molecules by Optical Tweezers

Published on: August 20, 2014

Probing RNA Structure with Dimethyl Sulfate Mutational Profiling with Sequencing In Vitro and in Cells

Probing RNA Structure with Dimethyl Sulfate Mutational Profiling with Sequencing In Vitro and in Cells

Published on: December 9, 2022

Area of Science:

Biochemistry
Molecular Biology
Structural Biology

Background:

Bovine pancreatic ribonuclease A (RNase A) is an enzyme that cleaves RNA.
RNase A possesses binding sites for various organic and inorganic molecules.
Ligand binding can modulate RNase A's secondary structure and catalytic function.

Purpose of the Study:

To investigate the effects of AZT (anti-AIDS), cis-Pt (antitumor), aspirin (anti-inflammatory), and vitamin C (antioxidant) on RNase A stability and conformation.
To compare the binding affinities and structural impacts of these diverse drug molecules on RNase A in vitro.

Main Methods:

UV-visible spectroscopy
Fourier-transform infrared (FTIR) spectroscopy
Circular dichroism (CD) spectroscopy

Main Results:

Binding affinities were determined for each drug-RNase A complex: KAZT=5.29x10(4) M(-1), Kaspirin=3.57x10(4) M(-1), Kcis-Pt=5.66x10(3) M(-1), and Kascorbate=3.50x10(3) M(-1).
Aspirin, vitamin C, and cis-Pt induced major protein unfolding, decreasing alpha-helix content from 29% to 20% and increasing beta-sheet content from 39% to 45%.
AZT binding resulted in a minor increase in alpha-helix content.

Conclusions:

The binding of AZT, cis-Pt, aspirin, and vitamin C significantly alters the secondary structure and stability of RNase A.
These conformational changes suggest potential modulation of RNase A's catalytic activity by these therapeutic agents.