By Gregg B. Fields (Eds.)

The significantly acclaimed laboratory regular for greater than 40 years, Methods in Enzymology is likely one of the such a lot hugely revered guides within the box of biochemistry. when you consider that 1955, each one volumehas been eagerly awaited, usually consulted, and praised by way of researchers and reviewers alike. greater than 275 volumes were released (all of them nonetheless in print) and masses of the cloth is correct even today-truly a necessary ebook for researchers in all fields of lifestyles sciences.

Key Features
* Solid-phase peptide synthesis
* purposes of peptides for structural and organic studies
* Characterization of man-made peptides

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Extra info for Solid-Phase Peptide Synthesis

Example text

7 The peptide-resin is soaked in a D M F solution of a palladium salt, 6j. M. Stewart and D. H. S. Patent 4,254,023 (1981). vM. K. Anwar, A. F. Spatola, C. D. Bossinger, E. Flanigan, R. C. Liu, D. B. Olsen, and D. Stevenson,J. Org. Chem. 8, 50 (1983). 34 METHODS FOR SOLID-PHASE ASSEMBLY OF PEPTIDES [3] and then ammonium formate is added to serve as hydrogen donor. One reported side reaction is saturation of the indole ring of Trp residues. Procedures for Peptide-Resin Cleavage Preparation of Peptide-Resin for Cleavage In preparation for cleavage, the Boc group should be removed by deprotection after coupling the last amino acid to minimize tert-butylation of susceptible residues (Tyr, Trp, Cys) in the product.

F. Alewood, Tetrahedron Len. 37, 4765 (1996). RAPID S P P S USING in Situ NEUTRALIZATION [2] 27 100 a 90 tx0 o 8O 70 6O N a, O 50 40 S I L E T K (C to N) I Y G T E T K (C to N) I Y G T 100 95 b 90 8s "~ 80 ~ 75 70 O Neutral = . 65 60 S I L FIG. 13. Chain assembly yields after 10 rain (a) and 1 hr (b) in the Fmoc synthesis of STAT91(699-709), TGYIKTELISV, using protocols 1 (Neutral) and 2 (In situ). this a r o s e w h e n , in t h e in situ a s s e m b l y o f a d i f f e r e n t e a s y s e q u e n c e , F m o c G l n ( T r t ) - O H was r e a d i l y i n c o r p o r a t e d with n o o b s e r v a b l e H B T U - d e r i v e d a d d u c t ( d a t a n o t shown).

5). Analysis by MS confirms that the major product contains the correct molecular weight (M r 2155). A minor product (Mr 71) is also present, a result of premature removal of the Acm protecting group during HF cleavage. Disulfide bond formation is carried out in two stages (Fig. 6). 0, 24 hr). The oxidized, di-Acm product is purified by reversed-phase (RP)-HPLC, and then the second disulfide bond is formed by removal of Acm with concurrent oxidation [I2 (10 equivalents) in 80/20 (v/v) acetic acid/water].

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