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Sequence context strongly modulates association of polar residues in transmembrane helices.
J Mol Biol
August 2003
Department of Molecular Biophysics and Biochemistry, Yale University, Bass Centre Room 420A, 266 Whitney Avenue, New Haven, CT 06520-8114, USA.
Article Synopsis
- Polar residues, like aspartic acid, asparagine, glutamic acid, and glutamine, can create hydrogen bonds between membrane-embedded helices, influencing their self-association.
- Research explored how these polar residues interact in various transmembrane domains, including naturally occurring proteins and modified bacteriophage proteins.
- Results showed that while some polar residues can stabilize interactions between helices, there are instances where they do not enhance association, indicating a complex control mechanism at play.