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Related Concept Videos

Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
Chair Conformation of Cyclohexane02:02

Chair Conformation of Cyclohexane

The chair conformation is the most stable form of cyclohexane due to the absence of angle and torsional strain. The absence of angle strain is a result of cyclohexane’s bond angle being very close to the ideal tetrahedral bond angle of 109.5° in its chair conformer. Similarly, the torsional strain is also absent owing to the perfectly staggered arrangement of bonds.
The hydrogen atoms linked to carbons are arranged in two different axial and equatorial orientations to achieve this staggered...
Conformations of Cyclohexane02:11

Conformations of Cyclohexane

Cyclohexane does not exist in a planar form due to the high angle and torsional strain it would experience in the planar structure. Instead, it adopts non-planar chair and boat conformations.
The chair form is the most stable and derives its name from its resemblance to the “easy chair.” In the chair conformation, two carbon atoms are arranged out-of-plane — one above and one below, minimizing the torsional strain. In the chair form, the bond angle is very close to the ideal tetrahedral value,...
¹H NMR of Conformationally Flexible Molecules: Temporal Resolution00:52

¹H NMR of Conformationally Flexible Molecules: Temporal Resolution

At room temperature, the chair conformer of cyclohexane undergoes rapid ring flipping between two equivalent chair conformers at a rate of approximately 105 times per second. These two chair conformers are in equilibrium. The rapid ring flipping results in the interconversion of the axial proton to an equatorial proton and an equatorial to the axial proton. Such interconversions are too rapid and cannot be detected on the NMR timescale. Hence, the NMR spectrometer cannot distinguish between the...
Protein Folding01:22

Protein Folding

Overview

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NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins
09:25

NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins

Published on: November 1, 2024

Conformational disorder.

Sonia Longhi1, Philippe Lieutaud, Bruno Canard

  • 1Architecture et Fonction des Macromolécules Biologiques, UMR 6098 CNRS et Universités Aix-Marseille I et II, Marseille, France.

Methods in Molecular Biology (Clifton, N.J.)
|March 12, 2010
PubMed
Summary
This summary is machine-generated.

Intrinsically disordered proteins lack a stable structure but perform vital functions. Identifying these disordered regions is crucial for protein annotation and understanding protein crystallization.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Bioinformatics

Background:

  • Proteins can be fully or partially disordered, lacking a stable 3D structure.
  • Intrinsically disordered proteins (IDPs) are abundant and perform essential biological functions.
  • Disordered regions are often difficult to detect, hindering functional annotation and domain boundary delineation.

Purpose of the Study:

  • To review current methods for predicting protein disorder.
  • To identify regions within proteins that are involved in induced folding.

Main Methods:

  • Focus on computational methods for disorder prediction.
  • Review of techniques for identifying regions prone to disorder-to-order transitions.

Main Results:

  • Disordered regions are prevalent in proteomes.
  • Accurate detection of disordered regions aids in functional annotation.
  • Identification of induced folding regions is key for crystallization.

Conclusions:

  • Improved prediction of intrinsically disordered proteins is essential.
  • Understanding disorder is critical for protein function and structural studies.
  • Methods for identifying disorder and induced folding regions advance biological research.