A biosensor study indicating that entropy, electrostatics, and receptor glycosylation drive the binding interaction between interleukin-7 and its receptor.

Walsh, Scott T R

Walsh, Scott T R.

Affiliation

Walsh ST; Department of Cell Biology and Molecular Genetics, Institute for Bioscience and Biotechnology Research, W. M. Keck Laboratory for Structural Biology, University of Maryland, 9600 Gudelsky Drive, Rockville, Maryland 20850, USA. swalsh12@umd.edu

Biochemistry ; 49(40): 8766-78, 2010 Oct 12.

Article in En | MEDLINE | ID: mdl-20815339

Subject(s)

Interleukin-7/metabolism; Receptors, Interleukin-7/metabolism; Biosensing Techniques; Entropy; Glycosylation; Humans; Interleukin-7/chemistry; Models, Molecular; Protein Binding; Protein Structure, Tertiary; Receptors, Interleukin-7/chemistry; Sodium Chloride/metabolism; Static Electricity

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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Interleukin-7 / Receptors, Interleukin-7 Limits: Humans Language: En Journal: Biochemistry Year: 2010 Type: Article Affiliation country: United States

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