Peptides reproducibility

Fig. 18 Peptide library used for studying complementary peptides. Reproduced from Takahashi et al. [57] with permission. Copyright Wiley-VCH...

Fig. 23 Sequences of various peptides and PEG-derivatised peptides. Reproduced with permission from Collier and Messersmith [68], Copyright Wiley-VCH...

Amino acids and peptides can be separated and their purity estimated rapidly and economically using TLC. In fact, until not long ago, TLC was to the peptide chemist what the hammer was to the carpenter, and extensive literature exists that describes all aspects of TLC including supports and solvent systems as well as the theory behind the separations. 4"14 TLC supports and solvent systems were developed since the beginning of this century to assess the purity of protected and unprotected amino acids and peptides reproducibly and quantitatively. 

Fia. 27. Effects of specific salts and of ionic strength on the C > p activity of RNase. (a) The activity is plotted as that observed relative to the value at low ionic strength (0.1 If). All C>p assays were carried out at pH 7. Insert Substrates, (0—0) RNA (pH 5.0) ( — ) C>p, salt, (NH,)2S04. (b) Effect of ammonium sulfate on the activity of various enzyme preparations (O) RNase-A, ( ) RNase-A (dimer), (A) RNase-S, (A) S-protein incubated with substrate and then activated with S-peptide. [Reproduced from Winstead and Wold (510).]... 

Figure 16.12 Structure of proinsulin, dark blocks representing the amino acids found in mature insulin. C peptide is the same as connecting peptide. (Reproduced by permission from Skillman T. Diabetes mellitus. In Kaplan A, Pesce AJ, eds. Clinical Chemistry. St. Louis CV Mosby, 1984, p. 526.)...

The CID ESI MS/MS spectrum of a doubly charged peptide. Reproduced from Finnigan MAT documentation, with permission. 

Figure 11 Formation of immonium ion and internal fragments. The immonium ions provide a clue to the composition of the peptide. Reproduced from C. Dass, Fundamentals of Contemporary Mass Spectrometry, Wiley-lnterscience Floboken, NJ, 2007, with permission from Wiley-lnterscience, Copyright 2007.

Figure 3.2 Steps in Edman degradation. The labeled aminoterminal residue (PTH -alanine in the first round) is released without hydrolyzing the remainder of the peptide. The cycle is repeated to reveal the complete sequence of the peptide. (Reproduced from Biochemistry by L. Stryer, K.B. Freeman, and company with the permission of the publisher.)...

Figure 1 Activation of Y3 receptors in the rat brainstem. (Top) Effects of NPY (90 pmol) injected into nucleus tractus solitarius on arterial pressure and heart rate in the anaesthetized rat. Characteristic of this receptor is that, in contrast to Y1 and Y2 receptors, it is not activated by PYY (90 pmol) (bottom). The black box indicates unilateral injection of peptide. Reproduced from Grundemar and Hakanson (1993) with permission.

Figure 18 The precatalytic complex of PHM with bound lYT peptide and dioxygen. The 2Fo-Fc electron density is shown for the lYT peptide. Reproduced from S. T. Prigge B. A. Eipper R. E. Mains L. M. Amzel, Science 2004, 304, 864-867, with permission from American Association for the Advancement of Science.

Figure 4.9 CD spectra of fixed concentration of plasmid DNA titrated with an increasing concentration of an adenoviral peptide, /x, known to template with DNA and induce condensation. Data illustrates that the peptide binding induces base-pair tilting and subsequent supercoiling (Chapters 1 and 7). Arrow shows direction of spectral increase with increasing /x peptide (Reproduced from Preuss et al., 2003, Fig. 4A).

Fig. 28.17 Schematic representation of the ball and chain model of channel inactivation. (A) The /V-termlnal sequence serves as an inactivation particle. (B) The effects of an A/-terminal peptide administered intraceiiularly on a mutant K channel lacking this terminal peptide. (Reproduced with permission from reference 108.)...

FIGURE 9.1 Schematic of microwave energy disrupting the aggregation in a peptide. (Reproduced with permission from Palasek, S. A. Cox, Z. J. Collins, J. M. J. Pept. Sci. 2007, 13, 143-148. Copyright John Wiley and Sons, Inc.)... 

FIGURE 9.3 Helical 3-peptide. (Reproduced with permission from Murray, J. K. Gellman, S. H. Org. Lett. 2005, 7, 1517-1520. Copyright American Chemical Society.)... 

Figure 3.4 Chemical structures of mPE and molecular models of AMP. For magainin (1), residues with hydrophilic (dark grey) and hydrophobic (light grey) side chains are on opposite sides of the helix, giving rise to an amphiphilic structure for PG-1 (2), the cationic amino acids (dark grey) flank both ends of the peptide. Reproduced with permission from Y. Ishitsuka, L. Arnt, J. Majewski, S. Frey, M. Ratajczek, K. Kjaer, G.N. Tew and K.Y.C. Lee, Journal of American Chemical Society, 2006,128,13123. 2006, American Chemical Society [43]...

FIGURE 1.9 Comparison of mass spectra derived from (a)CID andfbiETDofaphospho-peptide. (Reproduced from Syka, J.E.P. Coon, J.J. Schroeder, M.J. Shabanowitz, J. Hunt, D.F., Proc. Natl. Acad. Sci. USA. 2004, 101, 9528-9533. With permission from National Academy of Sciences.)... 

FIGURE 1,10 Product ion mass spectra of a tryptic lectin glycopeptide derived from (a) transmission mode ETD of the triply-charged peptide with azobenzene radical anions and (b) beam-type CID of the triply-charged peptide. (Reproduced from Han, H. Xia, Y. Yang, M. McLuckey, S.A., Anal. Chem. 2008, 80, 3492-3497. With permission from American Chemical Society.)... 

FIGURE 3.7 Proposed mechanism for the attachment of rhenate to a doubly-protonated peptide. (Reproduced from McAlister, G.C. Kiessel, S.E.B. Coon, J.J., Int. J. Mass Spectrom. 2008, 276, 149-152. With permission from Elsevier). 

SCHEME 4.2 Fixed-charge derivatization and selective gas-phase fragmentation of methionine fixed-charge sulfonium ion derivatized peptides. (Reproduced from Amunugama, M. Roberts, K.D. Reid, G.E., J. Am. Soc. Mass Spectrom. 2006,17,1631-1642. With permission from the American Society for Mass Spectrometry, published by Elsevier Inc.)... 

Figure 3.9. A Steps in the conversion of the gene product for insulin from preproinsulin to active (mature) insulin. B Space-filling representation of the active insulin molecule, as obtained from the crystal structure. C The ribbon model of active insulin showing the helical and extended regions of the A and B chains and the disulfide bridges that hold the A and B chains together after removal of the C peptide. (Reproduced with permission from Lehninger, Nelson, and Cox, Principles of Biochemistry, Second Edition, Worth Publishers.)...

Figure 15 Schematic drawing of a urea containing imprinted site complementary to the phosphotyrosine side chain of a phosphorylated peptide. (Reproduced from Ref. 39. Wiley-VCH, 2008.)...

Figure 22 Membrane fusion using model peptides designed by Marsden et al. (a) A schematic of how the model peptide constructs are designed to interact and form a heterodimer (b) A representation of peptide interactions in the natural system (c) A computer image of the two triblock copolymer constructs (d) A schematic of the fusion process with the model peptides. (Reproduced from Ref. 82. Wiley-VCH, 2009.)...

Y nitrotryrosine. C Cys-CAM. The bracket refers to the amino acid residue that preceded the N-terminus of the nitrated peptide. Reproduced from Zhan and Desiderio [19], with permission from Elsevier Science (USA), copyright 2004. 

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