Interdomain mobility and conformational stability of type III fibronectin domain pairs control surface adsorption, desorption and unfolding

Colloids and Surfaces B: Biointerfaces

Volumn 64, Issue 1, 2008, Pages 1-9

  Pereira, P ^a   Kelly, S M ^b   Gellert, P R ^c   van der Walle, C F ^a  

^a UNIVERSITY OF STRATHCLYDE   (United Kingdom)

^b UNIVERSITY OF GLASGOW   (United Kingdom)

^c ASTRAZENECA   (United Kingdom)

Author keywords

Circular dichroism; Surface adsorption; Total internal reflection fluorescence spectroscopy; Type III fibronectin domains

Indexed keywords

BIOMIMETICS; CELL ADHESION; CHEMICAL STABILITY; CONFORMATIONS; DICHROISM; FLUORESCENCE; FLUORESCENCE SPECTROSCOPY;

FIBRONECTIN DOMAINS; SURFACE ADSORPTION; TOTAL INTERNAL REFLECTION FLUORESCENCE SPECTROSCOPY;

GLYCOPROTEINS;

FIBRONECTIN; FIBRONECTIN 3;

ADSORPTION; ANALYTIC METHOD; ARTICLE; CIRCULAR DICHROISM; COMPARATIVE STUDY; CONFORMATION; DESORPTION; HYDROPHOBICITY; PRIORITY JOURNAL; PROTEIN SECONDARY STRUCTURE; SPECTROSCOPY; TOTAL INTERNAL REFLECTION FLUORESCENCE SPECTROSCOPY; WILD TYPE;

ADSORPTION; AMINO ACID SUBSTITUTION; FIBRONECTINS; HUMANS; PEPTIDE FRAGMENTS; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; SILICON DIOXIDE; SURFACE PROPERTIES;

EID: 43049084364     PISSN: 09277765     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.colsurfb.2007.12.015     Document Type: Article

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