Mapping Residual Structure in Intrinsically Disordered Proteins at Residue Resolution Using Millisecond Hydrogen/Deuterium Exchange and Residue Averaging (Q57958323)

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scientific article published in 2014

Language	Label	Description	Also known as
English	Mapping Residual Structure in Intrinsically Disordered Proteins at Residue Resolution Using Millisecond Hydrogen/Deuterium Exchange and Residue Averaging	scientific article published in 2014

Statements

scholarly article

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Mapping Residual Structure in Intrinsically Disordered Proteins at Residue Resolution Using Millisecond Hydrogen/Deuterium Exchange and Residue Averaging (English)

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protein structure

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object named as

David D. Weis

2

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author name string

Theodore R. Keppel

1

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publication date

7 December 2014

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Journal of the American Society for Mass Spectrometry

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26

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4

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547-554

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Intrinsic disorder and protein function

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https://api.crossref.org/works/10.1007%2FS13361-014-1033-6

21 January 2018

Intrinsically unstructured proteins and their functions

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Intrinsically Disordered Proteins in Human Diseases: Introducing the D 2 Concept

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Toward a quantitative theory of intrinsically disordered proteins and their function

1 reference

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Functional anthology of intrinsic disorder. 1. Biological processes and functions of proteins with long disordered regions.

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Linking folding and binding

1 reference

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21 January 2018

Hydrogen exchange and structural dynamics of proteins and nucleic acids

2 references

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21 January 2018

https://pubmed.ncbi.nlm.nih.gov/25481641

12 December 2020

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Hydrogen exchange mass spectrometry for studying protein structure and dynamics

1 reference

https://api.crossref.org/works/10.1007%2FS13361-014-1033-6

21 January 2018

Analysis of protein conformation and dynamics by hydrogen/deuterium exchange MS.

1 reference

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21 January 2018

Mapping unstructured regions and synergistic folding in intrinsically disordered proteins with amide H/D exchange mass spectrometry

1 reference

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Measuring dynamics in weakly structured regions of proteins using microfluidics-enabled subsecond H/D exchange mass spectrometry

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Time window expansion for HDX analysis of an intrinsically disordered protein

1 reference

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Analysis of disordered proteins using a simple apparatus for millisecond quench-flow H/D exchange

1 reference

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21 January 2018

Determination of amide hydrogen exchange by mass spectrometry: a new tool for protein structure elucidation

1 reference

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Electron capture dissociation of electrosprayed protein ions for spatially resolved hydrogen exchange measurements

1 reference

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Protein conformations can be probed in top-down HDX MS experiments utilizing electron transfer dissociation of protein ions without hydrogen scrambling.

1 reference

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Modeling deuterium exchange behavior of ERK2 using pepsin mapping to probe secondary structure.

1 reference

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Protein hydrogen exchange at residue resolution by proteolytic fragmentation mass spectrometry analysis

1 reference

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Improved protein hydrogen/deuterium exchange mass spectrometry platform with fully automated data processing

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Mutual synergistic folding in recruitment of CBP/p300 by p160 nuclear receptor coactivators

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NMR relaxation study of the complex formed between CBP and the activation domain of the nuclear hormone receptor coactivator ACTR.

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Random coil chemical shift for intrinsically disordered proteins: effects of temperature and pH.

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Modulation of the intrinsic helix propensity of an intrinsically disordered protein reveals long-range helix-helix interactions

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An Efficient and Inexpensive Refrigerated LC System for H/D Exchange Mass Spectrometry

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Primary structure effects on peptide group hydrogen exchange

1 reference

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Elucidating the folding problem of helical peptides using empirical parameters

1 reference

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Elucidating the folding problem of helical peptides using empirical parameters. II. Helix macrodipole effects and rational modification of the helical content of natural peptides.

1 reference

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Elucidating the folding problem of helical peptides using empirical parameters. III. Temperature and pH dependence.

1 reference

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Sequence complexity of disordered protein

1 reference

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Human recombinant [C22A] FK506-binding protein amide hydrogen exchange rates from mass spectrometry match and extend those from NMR

1 reference

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Computing H/D-exchange rates of single residues from data of proteolytic fragments.

1 reference

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21 January 2018

Helical structure and stability in human apolipoprotein A-I by hydrogen exchange and mass spectrometry

1 reference

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Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features

1 reference

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Temperature-dependent structural changes in intrinsically disordered proteins: formation of alpha-helices or loss of polyproline II?

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Hydrogen isotope exchange kinetics of single protons in bovine pancreatic trypsin inhibitor

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The 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data

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In-source fragmentation and the sources of partially tryptic peptides in shotgun proteomics.

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Structure and properties of alpha-synuclein and other amyloids determined at the amino acid level

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Peptide-column interactions and their influence on back exchange rates in hydrogen/deuterium exchange-MS.

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Hydrogen Exchange in Proteins

1 reference

https://pubmed.ncbi.nlm.nih.gov/25481641

12 December 2020

based on heuristic

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Measuring the hydrogen/deuterium exchange of proteins at high spatial resolution by mass spectrometry: overcoming gas-phase hydrogen/deuterium scrambling.

1 reference

https://pubmed.ncbi.nlm.nih.gov/25481641

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Isotope effects in peptide group hydrogen exchange

1 reference

https://pubmed.ncbi.nlm.nih.gov/25481641

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Hydrogen exchange-mass spectrometry: optimization of digestion conditions

1 reference

https://pubmed.ncbi.nlm.nih.gov/25481641

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1007/S13361-014-1033-6

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