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Structure determination of a protein assembly by amino acid selective cross-saturation

✍ Scribed by Eiji Kanamori; Shunsuke Igarashi; Masanori Osawa; Yoshifumi Fukunishi; Ichio Shimada; Haruki Nakamura

Book ID
105358160
Publisher
John Wiley and Sons
Year
2010
Tongue
English
Weight
599 KB
Volume
79
Category
Article
ISSN
0887-3585

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✦ Synopsis

Abstract

Amino acid selective cross‐saturation (ASCS) method not only provides information about the interface of a protein assembly by the spin relaxation experiment, but also identifies the amino acid residues in the acceptor protein, which are located close to the selectively labeled amino acid residues in the donor protein. Here, a new method was developed to build a precise structural model of a protein assembly, which satisfies the experimental ASCS values, using simulated annealing computation. This method was applied to the ubiquitin–yeast ubiquitin hydrolase 1 (Ub‐YUH1) complex to build a precise complex structure compatible with that determined by X‐ray crystallography. Proteins 2010. © 2010 Wiley‐Liss, Inc.

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