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Related Concept Videos

Protein Folding01:22

Protein Folding

Overview
Protein Folding01:25

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...
Lipids as Anchors01:32

Lipids as Anchors

In the plasma membrane, the lipids forming the bilayer can also act as an anchor to tether proteins to the membrane. The three main types of lipid anchors found in eukaryotes are – prenyl groups, fatty acyl groups, and glycosylphosphatidylinositol or GPI groups. Prenyl and fatty acyl groups act as anchors on the cytosolic surface of the membrane, whereas GPI anchors proteins on the extracellular side.
The carboxy-terminal of most of the prenylated proteins, such as Ras proteins, contains the...
Detergent Purification of Membrane Proteins01:18

Detergent Purification of Membrane Proteins

Detergents are used to purify the integral proteins of the membrane. The hydrophobic portion of the detergent can replace membrane phospholipids while solubilizing the membrane proteins. When detergent monomers reach a specific concentration in a solution called critical micelle concentration (CMC), they form micelles. Above CMC, the concentration of the detergent monomers remains in equilibrium with the micelle. The number of detergent monomers present in the CMC varies for each detergent, and...
Tail-anchoring of Proteins in the ER Membrane01:45

Tail-anchoring of Proteins in the ER Membrane

Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...
Globular Proteins01:27

Globular Proteins

In organisms, proteins are the most abundant macromolecules. They act as the building blocks of life and play various crucial roles in the body. Proteins can be broadly classified into two distinct subtypes based on their shape and solubilities: globular proteins and fibrous proteins.
Globular proteins serve many important physiological functions, such as acting as enzymes, cellular messengers, and molecular transporters. These roles often require the proteins to be soluble in the aqueous...

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Related Experiment Video

Updated: Jun 14, 2026

How to Stabilize Protein: Stability Screens for Thermal Shift Assays and Nano Differential Scanning Fluorimetry in the Virus-X Project
07:22

How to Stabilize Protein: Stability Screens for Thermal Shift Assays and Nano Differential Scanning Fluorimetry in the Virus-X Project

Published on: February 11, 2019

Golden rule for buttressing vulnerable soluble proteins.

Ariel Fernández1, R Stephen Berry

  • 1Department of Bioengineering, Rice University, Houston, Texas 77005, USA. arifer@rice.edu

Journal of Proteome Research
|April 7, 2010
PubMed
Summary

Structural weaknesses in proteins are often compensated by disulfide bonds. A new balance equation, Y = 5X + 20, reveals a 1:5 ratio critical for maintaining protein integrity and guiding biomolecular engineering.

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Last Updated: Jun 14, 2026

How to Stabilize Protein: Stability Screens for Thermal Shift Assays and Nano Differential Scanning Fluorimetry in the Virus-X Project
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Published on: August 14, 2011

Single Molecule Fluorescence Microscopy on Planar Supported Bilayers
20:00

Single Molecule Fluorescence Microscopy on Planar Supported Bilayers

Published on: October 31, 2015

Area of Science:

  • Biochemistry
  • Structural Biology
  • Protein Engineering

Background:

  • Local structural weaknesses in soluble proteins, often due to uncompensated backbone hydration costs, are poorly understood.
  • Intramolecular hydrogen bonds not stabilized by hydrophobic environments can compromise protein structural integrity.

Purpose of the Study:

  • To investigate the relationship between unburied backbone hydrogen bonds and disulfide bonds in soluble proteins.
  • To establish a quantitative relationship governing protein structural stability and identify key architectural constants.

Main Methods:

  • Analysis of a comprehensive dataset of Protein Data Bank (PDB)-reported soluble protein structures.
  • Statistical correlation and normalization techniques to quantify the relationship between unburied backbone hydrogen bonds (Y) and disulfide bonds (X).

Main Results:

  • A strong correlation was identified between the number of unburied backbone hydrogen bonds (Y) and disulfide bonds (X) in soluble proteins.
  • The relationship is accurately described by the equation Y = 5X + 20, indicating a baseline of 20 unburied hydrogen bonds and a 1:5 ratio for compensation.
  • This suggests disulfide bonds play a crucial role in buttressing proteins with structural deficiencies.

Conclusions:

  • Disulfide bonds are essential for maintaining the structural integrity of soluble proteins with uncompensated backbone hydration costs.
  • The derived equation and the 1:5 ratio provide universal constants applicable to understanding and engineering protein architecture.
  • Findings have significant implications for biomolecular engineering and protein design.