The critical role of the central hydrophobic core (residues 71-77) of amyloid-forming αA66-80 peptide in α-crystallin aggregation: a systematic proline replacement study.
Kannan, Rama
The critical role of the central hydrophobic core (residues 71-77) of amyloid-forming αA66-80 peptide in α-crystallin aggregation: a systematic proline replacement study. [electronic resource] - Amyloid : the international journal of experimental and clinical investigation : the official journal of the International Society of Amyloidosis Jun 2014 - 103-9 p. digital
Publication Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
1744-2818
10.3109/13506129.2014.888994 doi
Circular Dichroism
Hydrophobic and Hydrophilic Interactions
Microscopy, Electron, Transmission
Peptides--chemistry
Proline--chemistry
alpha-Crystallins--chemistry
The critical role of the central hydrophobic core (residues 71-77) of amyloid-forming αA66-80 peptide in α-crystallin aggregation: a systematic proline replacement study. [electronic resource] - Amyloid : the international journal of experimental and clinical investigation : the official journal of the International Society of Amyloidosis Jun 2014 - 103-9 p. digital
Publication Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
1744-2818
10.3109/13506129.2014.888994 doi
Circular Dichroism
Hydrophobic and Hydrophilic Interactions
Microscopy, Electron, Transmission
Peptides--chemistry
Proline--chemistry
alpha-Crystallins--chemistry