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Download PDF by Michael G. Rossmann (auth.), Alexander E. Kister (eds.): Protein Supersecondary Structures

By Michael G. Rossmann (auth.), Alexander E. Kister (eds.)

ISBN-10: 1627030646

ISBN-13: 9781627030649

ISBN-10: 1627030654

ISBN-13: 9781627030656

Super secondary structure(SSS) is helping to appreciate the connection among basic and tertiary constitution of proteins. In Protein Supersecondary constitution: equipment and Protocols professional researchers within the box aspect the usefulness of the examine of great secondary constitution in numerous parts of protein examine. this can be performed via 4 major reviews SSS illustration, SSS prediction, SSS and protein folding, and different software of SSS thought to protein biology. Written within the hugely winning Methods in Molecular Biology™ sequence structure, chapters contain introductions to their respective subject matters, lists of the mandatory fabrics and reagents, step by step, simply reproducible laboratory protocols, and key tips about troubleshooting and fending off identified pitfalls.

Authoritative and practical, Protein Supersecondary constitution: Methods and Protocols spotlight a number of the significant advances within the many fast-growing parts of supersecondary constitution research.

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In addition we outline methods to examine similarities and differences within and between the four stranded up-and-down blades of the β-propeller. Key words: Beta-propellers, Structural similarity, Classification, Beta sheet 1. Introduction The structure of a protein or a domain is described at increasing levels of complexity: primary, secondary, and tertiary structure. These descriptions are quite simple, but extensive: the sequence of amino acids, a list of hydrogen bonds between main chain atoms, and a list of atomic coordinates.

The term motif could then be used for a structural arrangement similar to a super-secondary structure, as judged by root mean square deviation. In a motif a secondary structural element could be missing or there could be additional secondary structural elements inserted between secondary structural elements of the super-secondary structure. For the description of the β-propellers below only a subset of blades display the up-and-down β-sheet super-secondary structure but all blades of the propeller have the up-and-down β-sheet motif since the fourth strand in many cases is not forming hydrogen bonds with strand 3.

28. 29. 30. 31. 32. 33. 34. 35. 36. 37. 33 for ligand binding in recombinant myoglobins. Thesis, Rice. 1. Proteins 78:917–931 Hohoff C, Borchers T, Rustow B et al (1999) Expression, purification, and crystal structure determination of recombinant human epidermal-type fatty acid binding protein. Biochemistry 38:12229–12239 Aghajari N, Feller G, Gerday C et al (1998) Crystal structures of the psychrophilic alphaamylase from Alteromonas haloplanctis in its native form and complexed with an inhibitor.

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Protein Supersecondary Structures by Michael G. Rossmann (auth.), Alexander E. Kister (eds.)


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