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

Pereira, P; Kelly, S M; Gellert, P R; van der Walle, C F

Pereira, P; Kelly, S M; Gellert, P R; van der Walle, C F.

Affiliation

Pereira P; Institute of Pharmacy and Biomedical Sciences, University of Strathclyde, 27 Taylor Street, Glasgow, UK.

Colloids Surf B Biointerfaces ; 64(1): 1-9, 2008 Jun 15.

Article in En | MEDLINE | ID: mdl-18261887

Subject(s)

Fibronectins/chemistry; Fibronectins/physiology; Peptide Fragments/chemistry; Peptide Fragments/physiology; Protein Conformation; Protein Folding; Adsorption; Amino Acid Substitution; Fibronectins/genetics; Humans; Peptide Fragments/genetics; Protein Structure, Tertiary; Silicon Dioxide; Surface Properties

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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Peptide Fragments / Protein Conformation / Fibronectins / Protein Folding Limits: Humans Language: En Journal: Colloids Surf B Biointerfaces Journal subject: QUIMICA Year: 2008 Document type: Article Affiliation country: United kingdom Country of publication: Netherlands

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