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

Protein Folding01:22

Protein Folding

117.5K
Overview
117.5K
Protein Organization01:24

Protein Organization

6.3K
Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence....
6.3K
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

17.8K
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...
17.8K
Protein and Protein Structure02:15

Protein and Protein Structure

78.8K
Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme...
78.8K
Amyloid Fibrils03:03

Amyloid Fibrils

9.3K
Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining,...
9.3K
¹H NMR: Interpreting Distorted and Overlapping Signals01:02

¹H NMR: Interpreting Distorted and Overlapping Signals

1.0K
Spin systems where the difference in chemical shifts of the coupled nuclei is greater than ten times J are called first-order spin systems. These nuclei are weakly coupled, and their chemical shifts and coupling constant can generally be estimated from the well-separated signals in the spectrum.
As Δν decreases and the signals move closer, the doublets appear increasingly distorted. The intensities of the inner lines increase at the cost of those of the outer lines as the signals are...
1.0K
  1. Home
  2. Research Domains
  3. Physical Sciences
  4. Condensed Matter Physics
  5. Surface Properties Of Condensed Matter
  6. Effective Patchiness From Critical Points Of A Coarse-grained Protein Model With Explicit Shape And Charge Anisotropy

Effective patchiness from critical points of a coarse-grained protein model with explicit shape and charge anisotropy

Jens Weimar1, Frank Hirschmann1, Martin Oettel1

  • 1Institute for Applied Physics, University of Tübingen, Auf der Morgenstelle 10, 72076 Tübingen, Germany. martin.oettel@uni-tuebingen.de.

Soft Matter
|October 14, 2024

Related Experiment Videos

Study of Protein Dynamics via Neutron Spin Echo Spectroscopy
08:03

Study of Protein Dynamics via Neutron Spin Echo Spectroscopy

Published on: April 13, 2022

2.0K
Analysis of SEC-SAXS data via EFA deconvolution and Scatter
10:59

Analysis of SEC-SAXS data via EFA deconvolution and Scatter

Published on: January 28, 2021

9.0K
A Protocol for Computer-Based Protein Structure and Function Prediction
16:41

A Protocol for Computer-Based Protein Structure and Function Prediction

Published on: November 3, 2011

68.6K

View abstract on PubMed

Summary
This summary is machine-generated.

Colloidal theory helps understand protein solutions, but anisotropic interactions require careful application of stability criteria. This study models bovine serum albumin (BSA) and finds charge anisotropy significantly impacts phase behavior.

Area of Science:

  • Colloid and soft matter physics
  • Computational biophysics
  • Protein science

Background:

  • Colloidal models explain protein solution behavior like aggregation and phase transitions.
  • Isotropic interaction models and the Noro-Frenkel rule are common for assessing solution stability.
  • Anisotropic protein interactions, like those in patchy particle models, alter stability criteria.

Purpose of the Study:

  • To investigate the effects of charge anisotropy on the phase diagram of a coarse-grained bovine serum albumin (BSA) model.
  • To develop methods for assigning effective patchiness to anisotropic protein models by comparing critical properties to the Kern-Frenkel model.
  • To assess the applicability of existing colloidal theory criteria to shape-anisotropic models.

Main Methods:

  • Utilized low-resolution, coarse-grained simulations to model bovine serum albumin (BSA).

Related Experiment Videos

Study of Protein Dynamics via Neutron Spin Echo Spectroscopy
08:03

Study of Protein Dynamics via Neutron Spin Echo Spectroscopy

Published on: April 13, 2022

2.0K
Analysis of SEC-SAXS data via EFA deconvolution and Scatter
10:59

Analysis of SEC-SAXS data via EFA deconvolution and Scatter

Published on: January 28, 2021

9.0K
A Protocol for Computer-Based Protein Structure and Function Prediction
16:41

A Protocol for Computer-Based Protein Structure and Function Prediction

Published on: November 3, 2011

68.6K
  • Determined the phase diagram of the BSA model at its isoelectric point.
  • Compared critical properties of the BSA model to the Kern-Frenkel (KF) patchy particle model to assign effective patchiness.
  • Main Results:

    • Doubling the native charges on the BSA model increased its critical temperature (Tc) by approximately 14%.
    • The simulated BSA model exhibited critical properties comparable to a 3 to 5 patch Kern-Frenkel model.
    • Normalization of the critical point criterion becomes ambiguous for shape-anisotropic models.

    Conclusions:

    • Charge anisotropy significantly influences the phase behavior and critical temperature of protein solutions.
    • Existing colloidal theory criteria for solution stability should be applied cautiously to shape-anisotropic models.
    • Defining effective diameters for anisotropic models requires careful consideration of multiple physically plausible assignments.