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Related Concept Videos

Amyloid Fibrils03:03

Amyloid Fibrils

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. 
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Amyloid Fibrils03:03

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Millisecond Hydrogen/Deuterium-Exchange Mass Spectrometry for the Study of Alpha-Synuclein Structural Dynamics Under Physiological Conditions
08:40

Millisecond Hydrogen/Deuterium-Exchange Mass Spectrometry for the Study of Alpha-Synuclein Structural Dynamics Under Physiological Conditions

Published on: June 23, 2022

Deamidation of alpha-synuclein.

Noah E Robinson1, Matthew L Robinson, Stephanie E S Schulze

  • 1Oregon Institute of Science and Medicine, Cave Junction, Oregon 97523, USA. noah@oism.org

Protein Science : a Publication of the Protein Society
|June 13, 2009
PubMed
Summary
This summary is machine-generated.

Alpha-synuclein deamidation, primarily at Asn103 and Asn122, occurs over 23 days. Sodium dodecyl sulfate (SDS) affects deamidation rates by altering protein structure, slowing N-terminal deamidation.

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LERLIC-MS/MS for In-depth Characterization and Quantification of Glutamine and Asparagine Deamidation in Shotgun Proteomics
08:01

LERLIC-MS/MS for In-depth Characterization and Quantification of Glutamine and Asparagine Deamidation in Shotgun Proteomics

Published on: April 9, 2017

Area of Science:

  • Biochemistry
  • Protein Chemistry
  • Mass Spectrometry

Background:

  • Protein deamidation is a post-translational modification affecting protein function.
  • Alpha-synuclein is implicated in neurodegenerative diseases, and its stability is crucial.
  • Understanding deamidation kinetics is vital for protein stability studies.

Purpose of the Study:

  • To quantify the deamidation rates of alpha-synuclein and its specific Asn residues.
  • To investigate the impact of sodium dodecyl sulfate (SDS) on deamidation kinetics.
  • To determine the influence of primary sequence and protein structure on deamidation.

Main Methods:

  • Utilized ion cyclotron resonance Fourier transform mass spectrometry for precise deamidation rate determination.
  • Employed an improved whole protein isotopic envelope method and a mass defect method.
  • Analyzed 13 Asn-sequence mutants and wild-type alpha-synuclein in the presence and absence of SDS.

Main Results:

  • Determined an overall deamidation half-time of 23 days for alpha-synuclein, mainly due to Asn103 and Asn122 deamidation.
  • Found deamidation rates were primarily sequence-controlled in the absence of SDS.
  • Observed that SDS micelles slowed deamidation rates for nine N-terminal Asn residues due to induced protein structures.

Conclusions:

  • Alpha-synuclein deamidation is a slow process influenced by specific residues and protein structure.
  • SDS binding induces conformational changes that modulate deamidation rates, particularly in the N-terminal region.
  • These findings provide insights into protein stability and modification relevant to alpha-synuclein's biological roles.