Aβ1-28 fragment of the amyloid peptide predominantly adopts a polyproline II conformation in an acidic solution

Biochemistry

Volumn 43, Issue 22, 2004, Pages 6893-6898

  Eker, Fatma ^a   Griebenow, Kai ^a   Schweitzer Stenner, Reinhard ^b  

^a UNIVERSITY OF PUERTO RICO   (Puerto Rico)

^b DREXEL UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

COMPUTER SIMULATION; DISEASES; FOURIER TRANSFORM INFRARED SPECTROSCOPY; MATHEMATICAL MODELS; RAMAN SCATTERING;

PEPTIDES; RANDOM-COIL STRUCTURE;

BIOCHEMISTRY;

AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN[1-28]; AMYLOID BETA PROTEIN[1-42]; POLYAMINOACID; POLYPROLINE II; PROLINE; UNCLASSIFIED DRUG; ACID; AMYLOID BETA PROTEIN (1 28); AMYLOID BETA-PROTEIN (1-28); PEPTIDE; PEPTIDE FRAGMENT; POLYPROLINE;

ALZHEIMER DISEASE; ARTICLE; FOURIER TRANSFORMATION; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; HUMAN; INFRARED SPECTROSCOPY; MODEL; NEUROLOGIC DISEASE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PEPTIDE ANALYSIS; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING; RAMAN SPECTROMETRY; CHEMISTRY; COMPARATIVE STUDY;

ACIDS; AMYLOID BETA-PROTEIN; HUMANS; PEPTIDE FRAGMENTS; PEPTIDES; PROTEIN CONFORMATION; PROTEIN FOLDING; SPECTROSCOPY, FOURIER TRANSFORM INFRARED; SPECTRUM ANALYSIS, RAMAN;

EID: 2642567722     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi049542+     Document Type: Article

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