Factors influencing compact-extended structure equilibrium in oligomers of aβ1-40 peptide - An ion mobility mass spectrometry study

Journal of Molecular Biology

Volumn 426, Issue 15, 2014, Pages 2871-2885

  Sitkiewicz, Ewa ^a   Kłoniecki, Marcin ^a   Poznański, Jarosław ^a   Bal, Wojciech ^a   Dadlez, Michał ^a,b  

^a INSTITUTE OF BIOCHEMISTRY AND BIOPHYSICS   (Poland)

^b UNIVERSITY OF WARSAW   (Poland)

Author keywords

Alzheimer's disease; A 1 40 peptide; collisional cross section; ion mobility separation mass spectrometry; oligomer structure

Indexed keywords

AMYLOID BETA PROTEIN[1-40]; METAL ION; OLIGOMER; SODIUM CHLORIDE;

ALZHEIMER DISEASE; ARTICLE; CONTROLLED STUDY; EVOLUTION; FIBER; HINGE REGION; HUMAN; INCUBATION TIME; ION MOBILITY SPECTROMETRY; MASS SPECTROMETRY; METAL BINDING; MOLECULAR DYNAMICS; MOLECULAR MODEL; NEUROTOXICITY; POINT MUTATION; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN EXPRESSION; PROTEIN STRUCTURE; REPRODUCIBILITY; SITE DIRECTED MUTAGENESIS; NONHUMAN; PROTEIN ANALYSIS;

ALZHEIMER'S DISEASE; AΒ1-40 PEPTIDE; COLLISIONAL CROSS-SECTION; ION MOBILITY SEPARATION MASS SPECTROMETRY; OLIGOMER STRUCTURE;

AMYLOID BETA-PEPTIDES; COPPER; HUMANS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; MUTATION; PEPTIDE FRAGMENTS; SPECTROMETRY, MASS, ELECTROSPRAY IONIZATION; ZINC SULFATE;

EID: 84904244209     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2014.05.015     Document Type: Article

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