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Related Concept Videos

Protein and Protein Structure02:15

Protein and Protein Structure

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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.
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Protein Complex Assembly02:41

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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.
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Molecular Chaperones and Protein Folding03:00

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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.
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Protein Complexes with Interchangeable Parts01:57

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Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
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¹H NMR of Conformationally Flexible Molecules: Temporal Resolution00:52

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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...
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Protein-protein Interfaces02:04

Protein-protein Interfaces

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Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
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Related Experiment Video

Updated: Feb 12, 2026

Isolation of Ribosome Bound Nascent Polypeptides in vitro to Identify Translational Pause Sites Along mRNA
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Isolation of Ribosome Bound Nascent Polypeptides in vitro to Identify Translational Pause Sites Along mRNA

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Conformational flexibility within the nascent polypeptide-associated complex enables its interactions with

Esther M Martin1, Matthew P Jackson1, Martin Gamerdinger2

  • 1From the Astbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds LS2 9JT, United Kingdom and.

The Journal of Biological Chemistry
|April 14, 2018
PubMed
Summary

The nascent polypeptide-associated complex (NAC) uses conformational flexibility to bind various unfolded or disordered proteins, preventing their aggregation. This chaperone

Keywords:
NAC native mass spectrometry (MS)chaperonemolecular chaperonenuclear magnetic resonance (NMR)protein cross-linkingprotein foldingprotein misfolding

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Using SecM Arrest Sequence as a Tool to Isolate Ribosome Bound Polypeptides
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Area of Science:

  • Molecular Biology
  • Biochemistry
  • Protein Folding

Background:

  • Newly synthesized polypeptides require correct folding to maintain protein homeostasis.
  • Ribosome-associated chaperones, like nascent polypeptide-associated complex (NAC), prevent premature protein aggregation.
  • The substrate-binding mechanism of NAC remains largely uncharacterized.

Purpose of the Study:

  • To investigate the conformational properties of Caenorhabditis elegans NAC.
  • To determine how NAC interacts with client proteins in different conformational states.
  • To elucidate the role of NAC in preventing protein aggregation, particularly of intrinsically disordered proteins.

Main Methods:

  • Native electrospray ionization mass spectrometry (ESI-MS)
  • Limited proteolysis
  • Nuclear Magnetic Resonance (NMR) spectroscopy
  • Cross-linking techniques

Main Results:

  • NAC exhibits a range of compact and expanded conformations.
  • NAC binds weakly to unfolded, folded, and intrinsically disordered proteins, indicating broad substrate compatibility.
  • This weak binding effectively retards the aggregation of α-synuclein both in vitro and in vivo.

Conclusions:

  • NAC possesses conformational plasticity enabling it to bind diverse substrates with unrelated sequences and structures.
  • NAC's function in preventing aggregation is independent of actively translating ribosomes.
  • These findings offer crucial insights into NAC's structure-function relationship and its role in protein quality control.