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

Globular and Fibrous Proteins

Globular and Fibrous Proteins

Many proteins can be classified into two distinct subtypes - globular or fibrous. These two types differ in their shapes and solubilities.
Globular proteins are also known as spheroproteins and typically are approximately round in shape. They contain a mix of amino acid types and contain differing sequences in their primary structures. Globular proteins have many different functions, such as enzymes, cellular messengers, and molecular transporters. These roles often require the proteins to be...

Gene Families

Gene Families

Gene families consist of groups of genes proposed to have originated from a common ancestor. Typically these arise through events in which a gene or genes are mistakenly duplicated during cell division. Unlike their parent genes (which are subject to selection pressure to maintain function), these gene copies do not need to preserve their sequences and may evolve at a relatively faster rate.
Occasionally these regions can be adapted to take on new roles within the organism, becoming novel genes...

SDS-PAGE

SDS-PAGE

Gel electrophoresis is a method that separates biological macromolecules like nucleic acids or proteins by forcing them to pass through a gel matrix under an electric field.
A variation of gel electrophoresis, termed polyacrylamide gel electrophoresis (PAGE), is commonly used for separating proteins according to their molecular size by passing them through a polyacrylamide gel. Because of the varying charges associated with amino acid side chains, PAGE can be used to separate intact proteins...

You might also read

Related Articles

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

Sort by

Same author

Black Hole Spectroscopy and Tests of General Relativity with GW250114.

Physical review letters·2026

Same author

GW250114: Testing Hawking's Area Law and the Kerr Nature of Black Holes.

Physical review letters·2025

Same author

The clinical and economic costs associated with regional disparities in varicella vaccine coverage in Italy over 50 years (2020-2070).

Scientific reports·2024

Same author

Quantum spin nematic phase in a square-lattice iridate.

Nature·2023

Same author

Frequency-Dependent Squeezed Vacuum Source for the Advanced Virgo Gravitational-Wave Detector.

Physical review letters·2023

Same author

A compact von Hámos spectrometer for parallel X-ray Raman scattering and X-ray emission spectroscopy at ID20 of the European Synchrotron Radiation Facility.

Journal of synchrotron radiation·2023

Search research articles

Related Experiment Video

Updated: May 29, 2026

Structural Studies of Macromolecules in Solution using Small Angle X-Ray Scattering

Structural Studies of Macromolecules in Solution using Small Angle X-Ray Scattering

Published on: November 5, 2018

SAXS study on myoglobin embedded in amorphous saccharide matrices.

S Giuffrida¹, M Panzica, F M Giordano

¹Dipartimento di Fisica, Università degli Studi di Palermo, via Archirafi 36, I-90123 Palermo, Italy. giuffrid@fisica.unipa.it

The European Physical Journal. E, Soft Matter

|September 23, 2011

Summary

Small Angle X-ray Scattering (SAXS) reveals inhomogeneities in myoglobin protein samples within various sugar matrices. These structural changes depend on sugar type, hydration, and reducing conditions, suggesting a general behavior in concentrated sugar environments.

More Related Videos

Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae

Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae

Published on: January 10, 2018

Related Experiment Videos

Last Updated: May 29, 2026

Structural Studies of Macromolecules in Solution using Small Angle X-Ray Scattering

Structural Studies of Macromolecules in Solution using Small Angle X-Ray Scattering

Published on: November 5, 2018

Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae

Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae

Published on: January 10, 2018

Area of Science:

Biophysics
Materials Science
Protein Chemistry

Background:

Myoglobin structure and function are sensitive to its environment.
Low-hydrated sugar matrices are used to stabilize proteins.
Previous studies suggested trehalose matrices induce inhomogeneities in myoglobin.

Purpose of the Study:

To investigate protein structural changes in different low-hydrated sugar matrices.
To determine if inhomogeneities are unique to trehalose or a general phenomenon.
To understand the influence of hydration and reducing agents on protein-sugar interactions.

Main Methods:

Small Angle X-ray Scattering (SAXS) measurements.
Analysis of carboxy-myoglobin and met-myoglobin.
Use of four saccharides: trehalose, sucrose, maltose, and lactose.
Controlled variations in sample hydration and presence of sodium dithionite.

Main Results:

Inhomogeneities were observed not only in trehalose but also in maltose and lactose matrices.
Sucrose matrices showed inhomogeneities in some cases.
The occurrence and extent of inhomogeneities were dependent on sample hydration levels.
The presence of sodium dithionite influenced the observed structural changes.

Conclusions:

Protein inhomogeneities in sugar matrices are not exclusive to trehalose.
These structural alterations represent a general behavior in highly concentrated sugar matrices.
Protein-sugar interactions and matrix properties significantly impact protein stability and structure.