Abstract
Deciphering how amino acid sequences direct polypeptide chains into their native folds remains a major unsolved problem. The most refractory aspect has been understanding the pathways and sequence control of β-sheet folding. This presumably reflects in part that residues that are far apart in the sequence will be intimately interacting in the folded β-structure.
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References
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King, J., Haase-Pettingell, C., Simkovsky, R., Weigele, P. (2005). Amino Acid Sequence Control of the Folding of the Parallel β-Helix, the Simplest β-Sheet Fold. In: Miyano, S., Mesirov, J., Kasif, S., Istrail, S., Pevzner, P.A., Waterman, M. (eds) Research in Computational Molecular Biology. RECOMB 2005. Lecture Notes in Computer Science(), vol 3500. Springer, Berlin, Heidelberg. https://doi.org/10.1007/11415770_35
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DOI: https://doi.org/10.1007/11415770_35
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-540-25866-7
Online ISBN: 978-3-540-31950-4
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