Antiparallel beta sheet

Fig. 19 Lateral model for assembly of peptide mixtures producing laminated P-sheets. Residues in solid circles are on the upper face, residues in dashed circles are on the lower face of the P-sheeL Reproduced from Takahashi et al. [57] with permission. Copyright Wiley-VCH. Numbers refer to the peptide entries in Fig. 18. Arrows are directions of the (antiparallel) beta sheet strands beginning and end of arrow correspond to N- and C-peptide termini respectively...

Petkova, A. T., Buntkowsky, G., Dyda, F., Leapman, R. D., Yau, W. M., and Tycko, R. (2004). Solid state NMR reveals a pH-dependent antiparallel beta-sheet registry in fibrils formed by a beta-amyloid peptide./. Mol. Biol. 335, 247-260. 

Griffiths-Jones SR, Searle MS. Stmcture, folding, and energetics of cooperative interactions between the beta-strands of a de novo designed three-stranded antiparallel beta-sheet peptide. J Am Chem Soc 2000 122 8350-8356. 

Fig. 3. Architecture of the kelch domain, (a) Stereoview of Domain II with the active site metal ion and protein ligands superimposed on a ribbon diagram of the polypeptide chain, (b) The modular organization of the sevenfold propeller domain is based on four-stranded antiparallel beta sheet subdomains.

Hendrix, J. C., Halverson, K. J., Jarrett, J. T., and Lansbury, P. T. (1990) A novel solvent system for solid-phase synthesis of protected peptides the disaggregation of resin-bound antiparallel beta-sheet. J. Org. Chem. 55, 4517-4518. 

The crystal structure of the active site of PARP has been described (5).It is made up of a five-stranded antiparallel beta sheet and a four-stranded mixed beta sheet (Fig. 11.2). The two beta sheets are connected by two hydrogen bonds. The beta sheet structure is supported by a surrounding protein structure made up of five alpha helices, three 3iq helices, and beta sheet excursions. The active site is... 

From the Ramachandran plot in Figure 3.35 of the text, we see that P conformation is accommodated by (j) values of approximately -140° and t / values of approximately -1-147°. The structure is most likely a P sheet. In fact, the low numbers here imply that it is an antiparallel beta sheet. The parallel P sheet would have higher numbers, more like (j) = -160° and t / = -f-160°. 

Demirdoven, N., Cheatum, CM., Chung, H.S., Khalil, M., Knoester, J. and Tokmakoff, A. (2004). Two-dimensional infrared spectroscopy of antiparallel beta-sheet secondary structure. Journal of the American Chemical Society, 126(25) 7981. doi 10.1021/ja049811j. PMID 15212548. 

Figure 21 compares the calculated structure of the isolated molecule, validated by cold ion spectroscopy, with that of the condensed-phase structure, solved by X-ray diffraction. The structures are similar, each containing a characteristic antiparallel beta-sheet motif. The near-symmetrical (C2) structure of the isolated. 

Viswanathan R, Asensio A, Dannenberg JJ (2004) Cooperative hydrogen-bonding in models of antiparallel beta-sheets. J Phys Chem A 108(42) 9205-9212. doi 10.1021/jp047404o... 

FIGURE 15 Examples o a + proteins, (a) Ubiquitin, (b) Papain consists of one alpha-helix and four strands of antiparallel beta-sheet, (c) ribonuclease A, and (d) N-terminal domain of E. co//glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase that contains a four structural layers appa. 

---