Search Results - "Heal, Jack W"

Characterization of Folding Cores in the Cyclophilin A-Cyclosporin A Complex by Heal, Jack W., Wells, Stephen A., Blindauer, Claudia A., Freedman, Robert B., Römer, Rudolf A.

“…Determining the folding core of a protein yields information about its folding process and dynamics. The experimental procedures for identifying the amino…”
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De novo protein design: how do we expand into the universe of possible protein structures? by Woolfson, Derek N, Bartlett, Gail J, Burton, Antony J, Heal, Jack W, Niitsu, Ai, Thomson, Andrew R, Wood, Christopher W

“…•The structural space explored by natural proteins is limited.•This raises questions: what protein folds are possible, and how do we access them?•Parametric…”
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Membrane-spanning α-helical barrels as tractable protein-design targets by Niitsu, Ai, Heal, Jack W., Fauland, Kerstin, Thomson, Andrew R., Woolfson, Derek N.

“…The rational (de novo) design of membrane-spanning proteins lags behind that for water-soluble globular proteins. This is due to gaps in our knowledge of…”
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ISAMBARD: an open-source computational environment for biomolecular analysis, modelling and design by Wood, Christopher W, Heal, Jack W, Thomson, Andrew R, Bartlett, Gail J, Ibarra, Amaurys Á, Brady, R Leo, Sessions, Richard B, Woolfson, Derek N

“…The rational design of biomolecules is becoming a reality. However, further computational tools are needed to facilitate and accelerate this, and to make it…”
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Engineering protein stability with atomic precision in a monomeric miniprotein by Baker, Emily G, Williams, Christopher, Hudson, Kieran L, Bartlett, Gail J, Heal, Jack W, Porter Goff, Kathryn L, Sessions, Richard B, Crump, Matthew P, Woolfson, Derek N

“…The design and mutagenesis of an α-helix-containing monomeric miniprotein, PPα-Tyr, provide insights into weak noncovalent CH–π interactions that help define…”
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Applying graph theory to protein structures: an Atlas of coiled coils by Heal, Jack W, Bartlett, Gail J, Wood, Christopher W, Thomson, Andrew R, Woolfson, Derek N

“…Abstract Motivation To understand protein structure, folding and function fully and to design proteins de novo reliably, we must learn from natural protein…”
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‘Something in the way she moves’: The functional significance of flexibility in the multiple roles of protein disulfide isomerase (PDI) by Freedman, Robert B., Desmond, Jasmine L., Byrne, Lee J., Heal, Jack W., Howard, Mark J., Sanghera, Narinder, Walker, Kelly L., Wallis, A. Katrine, Wells, Stephen A., Williamson, Richard A., Römer, Rudolf A.

“…Protein disulfide isomerase (PDI) has diverse functions in the endoplasmic reticulum as catalyst of redox transfer, disulfide isomerization and oxidative…”
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Does deamidation cause protein unfolding? A top-down tandem mass spectrometry study by Soulby, Andrew J, Heal, Jack W, Barrow, Mark P, Roemer, Rudolf A, O'Connor, Peter B

“…Deamidation is a nonenzymatic post-translational modification of asparagine to aspartic acid or glutamine to glutamic acid, converting an uncharged amino acid…”
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Membrane-spanning α-helical barrels as tractable protein-design targets by Niitsu, Ai, Heal, Jack W., Fauland, Kerstin, Thomson, Andrew R., Woolfson, Derek N.

“…The rational (de novo) design of membrane-spanning proteins lags behind that for water-soluble globular proteins. This is due to gaps in our knowledge of…”
Get full text