The induction of α-helical structure in partially unfolded HypF-N does not affect its aggregation propensity

Protein Engineering, Design and Selection

Volumn 24, Issue 7, 2011, Pages 553-563

  Ahmad, B ^a,d   Vigliotta, I ^a   Tatini, F ^a   Campioni, S ^a,e   Mannini, B ^a   Winkelmann, J ^a   Tiribilli, B ^b   Chiti, F ^a,c  

^a UNIVERSITY OF FLORENCE   (Italy)

^b ISTITUTO DEI SISTEMI COMPLESSI   (Italy)

^c NATIONAL INSTITUTE OF BIOSTRUCTURES AND BIOSYSTEMS   (Italy)

^d MICHIGAN STATE UNIVERSITY   (United States)

^e ETH ZURICH   (Switzerland)

Author keywords

helical intermediate; aggregation mechanism; amyloid fibrils; on pathway; protein misfolding

Indexed keywords

ACCELERATING EFFECT; AGGREGATION MECHANISM; AGGREGATION PROPENSITY; AGGREGATION RATE; AMYLOID FIBRIL; BIOLOGY AND MEDICINE; CENTRAL PROBLEMS; CONFORMATIONAL STATE; DYNAMIC STATE; FIBRILLAR AGGREGATES; HELICAL STRUCTURES; ON-PATHWAY; PROTEIN AGGREGATION; PROTEIN CHEMISTRY; PROTEIN MISFOLDING; PROTEIN SYSTEM; RESIDUAL STRUCTURE; STRUCTURAL ELEMENTS;

PEPTIDES;

CONFORMATIONS;

AMYLOID PROTEIN; ESCHERICHIA COLI PROTEIN; PEPTIDE; PROTEIN HYPF N; UNCLASSIFIED DRUG;

ALPHA HELIX; ARTICLE; CONTROLLED STUDY; HUMAN; HYDROPHOBICITY; MUTATION; NONHUMAN; PH; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN CONFORMATION; PROTEIN STRUCTURE; PROTEIN UNFOLDING; SEQUENCE ANALYSIS;

CARBOXYL AND CARBAMOYL TRANSFERASES; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; HYDROGEN-ION CONCENTRATION; MODELS, MOLECULAR; MUTATION; PROTEIN STABILITY; PROTEIN STRUCTURE, SECONDARY; PROTEIN UNFOLDING;

EID: 79959741796     PISSN: 17410126     EISSN: 17410134     Source Type: Journal    
DOI: 10.1093/protein/gzr018     Document Type: Article

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