Protein cont

I. Amino Acids Found in Most Proteins— Cont d JfydrophiHc Amino Acids Uncharged Polar Groups- onfd... 

CA Orengo, EMC Pearl, JE Bray, AE Todd, AC Martin, L Lo Conte, JM Thornton. The GATH database provides insights into protein stmcture/function relationship. Nucleic Acids Res 27 275-279, 1999. 

TF Smith, L Lo Conte, J Bienkowska, C Gaitatzes, RGJ Rogers, R Lathrop. CuiTent limitations to protein threading approaches. J Comput Biol 4 217-225, 1997. 

TABLE 23-3 Examples of proteins regulated by phosphorylation— cont d... 

Lo Conte, L., Chothia, C and Janin, J. (1999) The atomic structure of protein-protein recognition sites../. Mol. Biol. 285,2177-2198. 

Correct answer D. in proteins found in aqueous solutions, the side chains ot the nonpolar amino acids,. tfi. otoucme tend to duster together in the interior of the protein. G -nmeiecontans an amide in its side chains. Seme and threonine contains a hydroxyl group in their side chain. Cysteine can form (teUfide bonds. Gtyune conte s the smalest side chain. 

Table 10.1. Summary of platyhelminth signalling proteins for which molecular evidence is available. (cont d)...

The Protein Data Bank (PDB) is the primary structure database serving as the international repository for the processing and distribution of 3D structures of biomacromolecules (Bernstein et al, 1977). The database is operated by the Research Collaboratory for Structural Bioinformatics (RCSB) and is accessible from the primary RCSB site at http //www.rcsb.org/pdb/ (Berman et al., 2000). Most of the structure fold/motif/domain databases (Conte et al., 2000) and analysis servers (Brenner et al, 2000 Hofmann et al, 2000 Kelley et al., 2000 Shi et al., 2001) utilize 3D-structure information from PDB and sequence information from primary sequence databases. Some of these databases/analysis servers and their URL are listed in Table 12.3. 

In the most comprehensive structural analysis to date, Lo Conte et al.11 studied 75 protein-protein complexes comprising 24 protease-inhibitor, 19 antibody-antigen, and 32 other complexes (including 9 further enzyme-inhibitor and 11 signal transduction complexes). The authors found that protein-protein interfaces typically have a size of 1600 400 A2 with a few complexes exhibiting very large (2000—4660 A2) or very small (less than 1000 A2) interfaces. With respect to their chemical nature, the interfaces were found to... 

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