Self-association of model transmembrane alpha-helices is modulated by lipid structure.

Mall, S; Broadbridge, R; Sharma, R P; East, J M; Lee, A G

Mall, S; Broadbridge, R; Sharma, R P; East, J M; Lee, A G.

Affiliation

Mall S; Division of Biochemistry and Molecular Biology, School of Biological Sciences, University of Southampton, Southampton SO16 7PX, UK.

Biochemistry ; 40(41): 12379-86, 2001 Oct 16.

Article in En | MEDLINE | ID: mdl-11591157

Subject(s)

Lipid Bilayers/chemistry; Membrane Proteins/chemistry; Amino Acid Sequence; Dimerization; Fluorescence; Gels; In Vitro Techniques; Membranes, Artificial; Models, Molecular; Peptides/chemistry; Protein Structure, Secondary; Thermodynamics; Tyrosine/analogs & derivatives; Tyrosine/chemistry

Search on Google

Add to My VHL

XML

PubMed Links

Collection: 01-internacional Database: MEDLINE Main subject: Lipid Bilayers / Membrane Proteins Type of study: Risk_factors_studies Language: En Journal: Biochemistry Year: 2001 Document type: Article Affiliation country: United kingdom Country of publication: United States

Search on Google

Add to My VHL

XML

PubMed Links