Probing high order structure of proteins by fast-atom bombardment mass spectrometry (Q47722508)

5 February 2018

title

Probing high order structure of proteins by fast-atom bombardment mass spectrometry (English)

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5 February 2018

author name string

Y Liu

series ordinal

1

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5 February 2018

D L Smith

series ordinal

2

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5 February 2018

publication date

1 January 1994

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5 February 2018

Journal of the American Society for Mass Spectrometry

published in

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5 February 2018

volume

5

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5 February 2018

issue

1

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5 February 2018

page(s)

19-28

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5 February 2018

Solvent-induced conformational changes of polypeptides probed by electrospray-ionization mass spectrometry

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Structural description of acid-denatured cytochrome c by hydrogen exchange and 2D NMR.

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An Antibody Binding Site on Cytochrome C Defined by Hydrogen Exchange and Two-Dimensional NMR

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Hydrogen--tritium exchange

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Membrane binding induces destabilization of cytochrome c structure.

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Protein hydrogen exchange studied by the fragment separation method.

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Hydrogen exchange measurement of the free energy of structural and allosteric change in hemoglobin.

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

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Improved resolution of calf lens β-crystallins

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The Amino-Acid Sequence of the alphaB2 Chain of Bovine alpha-Crystallin

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Elucidation of the primary structures of proteins by mass spectrometry

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A dynamic quaternary structure of bovine alpha-crystallin as indicated from intermolecular exchange of subunits.

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Biophysical characterization of alpha-crystallin aggregates: validation of the micelle hypothesis

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Hydrogen exchange and structural dynamics of proteins and nucleic acids

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12 December 2020

based on heuristic

Primary structure effects on peptide group hydrogen exchange.

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Measurement and calibration of peptide group hydrogen-deuterium exchange by ultraviolet spectrophotometry

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Probing qualitative conformation differences of multiply protonated gas-phase proteins via hydrogen/deuterium isotopic exchange with water-d2

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Mass spectrometric analysis of lens β-crystallins

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Hydrogen exchange kinetics of bovine pancreatic trypsin inhibitor beta-sheet protons in trypsin-bovine pancreatic trypsin inhibitor, trypsinogen-bovine pancreatic trypsin inhibitor, and trypsinogen-isoleucylvaline-bovine pancreatic trypsin inhibitor

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Effects of denaturants on amide proton exchange rates: a test for structure in protein fragments and folding intermediates

21 January 2018

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Hydrogen exchange from identified regions of the S-protein component of ribonuclease as a function of temperature, pH, and the binding of S-peptide

21 January 2018

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Spectroscopic investigations of bovine lens crystallins. 1. Circular dichroism and intrinsic fluorescence

21 January 2018

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Determination of amide hydrogen exchange rates in peptides by mass spectrometry

21 January 2018

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Micellar subunit assembly in a three-layer model of oligomeric alpha-crystallin.

21 January 2018

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PubMed

https://pubmed.ncbi.nlm.nih.gov/24226137

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Identifiers

DOI

10.1016/1044-0305(94)85080-1

1 reference

5 February 2018

Dimensions Publication ID

1015683610

0 references

1 reference

5 February 2018