Human islet amyloid polypeptide at the air-aqueous interface: A Langmuir monolayer approach

Journal of the Royal Society Interface

Volumn 9, Issue 76, 2012, Pages 3118-3128

  Li, Shanghao ^a   Micic, Miodrag ^b,c   Orbulescu, Jhony ^b   Whyte, Jeffrey D ^b   Leblanc, Roger M ^a  

^a University of Miami   (United States)

^b MP Biomedicals LLC   (United States)

^c Irvine   (United States)

Author keywords

hIAPP; Langmuir monolayer; Orientation; Protein; Stability

Indexed keywords

AGGLOMERATION; AGGREGATES; CONVERGENCE OF NUMERICAL METHODS; CRYSTAL ORIENTATION; FLUORESCENCE SPECTROSCOPY; GLYCOPROTEINS; MONOLAYERS; PROTEINS; SODIUM CHLORIDE;

AGGREGATION PROCESS; AMYLOID DEPOSITS; BREWSTER ANGLE MICROSCOPY; DIABETIC PATIENT; HELIX CONFORMATION; HIAPP; HUMAN ISLETS; ISLETS OF LANGERHANS; LANGMUIR MONOLAYERS; P-POLARIZED; PARALLEL ORIENTATION; SECONDARY STRUCTURES; SUBPHASES; SURFACE PRESSURES; UV-VIS ABSORPTIONS;

PHASE INTERFACES;

AMYLIN; SODIUM CHLORATE;

ABSORPTION SPECTROSCOPY; AIR; ALPHA HELIX; AQUEOUS SOLUTION; ARTICLE; BREWSTER ANGLE MICROSCOPY; FLUORESCENCE SPECTROSCOPY; INFRARED RADIATION; INTERFACE PRESSURE; ISOTHERM; MONOLAYER CULTURE; PH; POLARIZATION; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTEIN SECONDARY STRUCTURE; ULTRAVIOLET SPECTROSCOPY;

EID: 84867439685     PISSN: 17425689     EISSN: 17425662     Source Type: Journal    
DOI: 10.1098/rsif.2012.0368     Document Type: Article

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