15N CEST data and traditional model-free analysis capture fast internal dynamics of DJ-1

Jonathan Catazaro, Tessa Andrews, Nicole M. Milkovic, Jiusheng Lin, Austin J. Lowe, Mark A. Wilson, Robert Powers

Research output: Contribution to journalArticle

Abstract

Previous studies have shown that relaxation parameters and fast protein dynamics can be quickly elucidated from 15N-CEST experiments [1]. Longitudinal R1 and transverse R2 values were reliably derived from fitting of CEST profiles. Herein we show that 15N-CEST experiments and traditional modelfree analysis provide the internal dynamics of three states of human protein DJ-1 at physiological temperature. The chemical exchange profiles show the absence of a minor state conformation and, in conjunction with 1H-15N NOEs, show increased mobility. R1 and R2 values remained relatively unchanged at the three naturally occurring oxidation states of DJ-1, but exhibit striking NOE differences. The NOE data was, therefore, essential in determining the internal motions of the DJ-1 proteins. To the authors' knowledge, we present the first study that combines 15N CEST data with traditional model-free analyses in the study of a biological system and affirm that more ‘lean’ model-free approaches should be used cautiously.

LanguageEnglish (US)
Pages24-28
Number of pages5
JournalAnalytical Biochemistry
Volume542
DOIs
StatePublished - Feb 1 2018

Fingerprint

Temperature
Biological systems
Conformations
Proteins
Experiments
Oxidation
Protein Deglycase DJ-1
human PARK7 protein

Keywords

  • CEST
  • DJ-1
  • NMR
  • Protein dynamics

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

15N CEST data and traditional model-free analysis capture fast internal dynamics of DJ-1. / Catazaro, Jonathan; Andrews, Tessa; Milkovic, Nicole M.; Lin, Jiusheng; Lowe, Austin J.; Wilson, Mark A.; Powers, Robert.

In: Analytical Biochemistry, Vol. 542, 01.02.2018, p. 24-28.

Research output: Contribution to journalArticle

Catazaro, Jonathan ; Andrews, Tessa ; Milkovic, Nicole M. ; Lin, Jiusheng ; Lowe, Austin J. ; Wilson, Mark A. ; Powers, Robert. / 15N CEST data and traditional model-free analysis capture fast internal dynamics of DJ-1. In: Analytical Biochemistry. 2018 ; Vol. 542. pp. 24-28.
@article{aa4410c2c33d4358a9bbc72179a0143a,
title = "15N CEST data and traditional model-free analysis capture fast internal dynamics of DJ-1",
abstract = "Previous studies have shown that relaxation parameters and fast protein dynamics can be quickly elucidated from 15N-CEST experiments [1]. Longitudinal R1 and transverse R2 values were reliably derived from fitting of CEST profiles. Herein we show that 15N-CEST experiments and traditional modelfree analysis provide the internal dynamics of three states of human protein DJ-1 at physiological temperature. The chemical exchange profiles show the absence of a minor state conformation and, in conjunction with 1H-15N NOEs, show increased mobility. R1 and R2 values remained relatively unchanged at the three naturally occurring oxidation states of DJ-1, but exhibit striking NOE differences. The NOE data was, therefore, essential in determining the internal motions of the DJ-1 proteins. To the authors' knowledge, we present the first study that combines 15N CEST data with traditional model-free analyses in the study of a biological system and affirm that more ‘lean’ model-free approaches should be used cautiously.",
keywords = "CEST, DJ-1, NMR, Protein dynamics",
author = "Jonathan Catazaro and Tessa Andrews and Milkovic, {Nicole M.} and Jiusheng Lin and Lowe, {Austin J.} and Wilson, {Mark A.} and Robert Powers",
year = "2018",
month = "2",
day = "1",
doi = "10.1016/j.ab.2017.11.012",
language = "English (US)",
volume = "542",
pages = "24--28",
journal = "Analytical Biochemistry",
issn = "0003-2697",
publisher = "Academic Press Inc.",

}

TY - JOUR

T1 - 15N CEST data and traditional model-free analysis capture fast internal dynamics of DJ-1

AU - Catazaro, Jonathan

AU - Andrews, Tessa

AU - Milkovic, Nicole M.

AU - Lin, Jiusheng

AU - Lowe, Austin J.

AU - Wilson, Mark A.

AU - Powers, Robert

PY - 2018/2/1

Y1 - 2018/2/1

N2 - Previous studies have shown that relaxation parameters and fast protein dynamics can be quickly elucidated from 15N-CEST experiments [1]. Longitudinal R1 and transverse R2 values were reliably derived from fitting of CEST profiles. Herein we show that 15N-CEST experiments and traditional modelfree analysis provide the internal dynamics of three states of human protein DJ-1 at physiological temperature. The chemical exchange profiles show the absence of a minor state conformation and, in conjunction with 1H-15N NOEs, show increased mobility. R1 and R2 values remained relatively unchanged at the three naturally occurring oxidation states of DJ-1, but exhibit striking NOE differences. The NOE data was, therefore, essential in determining the internal motions of the DJ-1 proteins. To the authors' knowledge, we present the first study that combines 15N CEST data with traditional model-free analyses in the study of a biological system and affirm that more ‘lean’ model-free approaches should be used cautiously.

AB - Previous studies have shown that relaxation parameters and fast protein dynamics can be quickly elucidated from 15N-CEST experiments [1]. Longitudinal R1 and transverse R2 values were reliably derived from fitting of CEST profiles. Herein we show that 15N-CEST experiments and traditional modelfree analysis provide the internal dynamics of three states of human protein DJ-1 at physiological temperature. The chemical exchange profiles show the absence of a minor state conformation and, in conjunction with 1H-15N NOEs, show increased mobility. R1 and R2 values remained relatively unchanged at the three naturally occurring oxidation states of DJ-1, but exhibit striking NOE differences. The NOE data was, therefore, essential in determining the internal motions of the DJ-1 proteins. To the authors' knowledge, we present the first study that combines 15N CEST data with traditional model-free analyses in the study of a biological system and affirm that more ‘lean’ model-free approaches should be used cautiously.

KW - CEST

KW - DJ-1

KW - NMR

KW - Protein dynamics

UR - http://www.scopus.com/inward/record.url?scp=85034866436&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85034866436&partnerID=8YFLogxK

U2 - 10.1016/j.ab.2017.11.012

DO - 10.1016/j.ab.2017.11.012

M3 - Article

VL - 542

SP - 24

EP - 28

JO - Analytical Biochemistry

T2 - Analytical Biochemistry

JF - Analytical Biochemistry

SN - 0003-2697

ER -