By David A.D. Parry, John M. Squire
This ebook presents the readers with an up to date overview of the layout, constitution and serve as of a consultant collection of fibrous proteins in either healthiness and disorder. the significance of the α-helical coiled coil, a conformational motif in response to the heptad repeat within the amino acid series of all α-fibrous proteins (and components of a few globular proteins) is underlined by way of 3 Chapters dedicated to its layout, constitution, functionality and topology. particular proteins coated within the textual content and which depend upon the coiled coil for his or her constitution and serve as, contain the intermediate filament proteins, tropomyosin, myosin, paramyosin, fibrin and contributors of the spectrin superfamily. additionally defined are fibrous proteins in accordance with the β-pleated sheet and collagen conformations. Recombinant structural proteins, particularly of silk and collagen, are mentioned within the context of constructing new biomaterials with assorted purposes.
Established researchers and postgraduate scholars within the fields of protein chemistry, biochemistry and structural biophysics will locate Fibrous Proteins: constructions and Mechanisms to be a useful selection of topical stories that describe the fundamental advances made within the box of fibrous proteins during the last decade. This ebook, written through well-known experts within the box, presents a transparent account of the present prestige of fibrous protein examine and, additionally, establishes the foundation for determining the main acceptable instructions for destiny task, together with the purposes of protein engineering and the economic exploitation of recent biomaterials.
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Additional resources for Fibrous Proteins: Structures and Mechanisms
Because the field has developed considerably over the past 10 years, this new review has been structured differently. Firstly, what can be and has been achieved using established and relatively straightforward sequence-to-structure relationships in classical coiled coils is summarised. Secondly, there is a discussion of how the field is moving on in 2 Coiled-Coil Design 37 terms of understanding coiled-coil sequences and structures more generally. This requires us to adjust and expand our traditional view of the sequence repeats and helix packing.
Increasing the helix-helix contacts in pentamers and above leads to Type II interfaces, in which sidechains at both g and e sites are involved in KIH interactions, Fig. 7c. For completeness, Type III interfaces are the final variations in this scheme, and these lead to barrels of the type observed in the 12-helix barrel of TolC, Fig. 7d (Koronakis et al. 2000; Walshaw and Woolfson 2001a). Another way to consider this is that coiled-coil pentamers and above comprise two superposed dimer sequences with the two traditional a and d hydrophobic seams falling at e and a, and d and g positions, respectively, Fig.
Proc Natl Acad Sci U S A 37:729–740 1 Fibrous Protein Structures: Hierarchy, History and Heroes 33 Pauling L, Corey RB (1953a) Compound helical configurations of polypeptide chains: structure of proteins of the alpha-keratin type. Nature 171:59–61 Pauling L, Corey RB (1953b) Two rippled-sheet configurations of polypeptide chains, and a note about the pleated sheets. Proc Natl Acad Sci U S A 39:253–256 Pauling L, Corey RB, Branson HR (1951) The structure of proteins; two hydrogen-bonded helical configurations of the polypeptide chain.