Proline forms

This group was developed for the protection of amino acids. It is formed from 4-ethoxy-l,l,l-trifluoro-3-buten-2-one in aqueous sodium hydroxide (70-94% yield). Primary amino acids form the Z-enamines, whereas secondary amines such as proline form the -enamines. Deprotection is achieved with 1-6 N aqueous HCl in dioxane at rt. ... 

N 032 "Conformational Properties of Poly(L-proline) Form II in Dilute Solution"... 

It is well-known that catalytic amounts of aldehyde can induce racemization of a-amino acids through the reversible formation of Schiff bases.61 Combination of this technology with a classic resolution leads to an elegant asymmetric transformation of L-proline to D-proline (Scheme 6.8).62 63 When L-proline is heated with one equivalent of D-tartaric acid and a catalytic amount of n-butyraldehyde in butyric acid, it first racemizes as a result of the reversible formation of the proline-butyraldehyde Schiff base. The newly generated D-proline forms an insoluble salt with D-tartaric acid and precipitates out of the solution, whereas the soluble L-proline is continuously being racemized. The net effect is the continuous transformation of the soluble L-proline to the insoluble D-proline-D-tartaric acid complex, resulting in near-complete conversion. Treatment of the D-proline-D-tartaric acid complex with concentrated ammonia in methanol liberates the D-proline (16) (99% ee, with 80-90% overall yield from L-proline). This is a typical example of a dynamic resolution where L-proline is completely converted to D-proline with simultaneous in situ racemization. As far as the process is concerned, this is an ideal case because no extra step is required for recycle and racemization of the undesired enantiomer and a 100% chemical yield is achievable. The only drawback of this process is the use of stoichiometric amount of D-tartaric acid, which is the unnatural form of tartaric acid and is relatively expensive. Fortunately, more than 90% of the D-tartaric acid is recovered at the end of the process as the diammonium salt that can be recycled after conversion to the free acid.64... 

Experiments conducted in the mid-1980s by Agami indicated a small nonlinear effect in the asymmetric catalysis in the Hajos-Parrish-Wiechert-Eder-Sauer reaction (Scheme 6.7). Agami proposed that two proline molecules were involved in the catalysis the first proline forms an enamine with the side chain ketone and the second proline molecule facilitates a proton transfer. Hajos and Parrish reported that the proline-catalyzed cyclization shown in Scheme 6.7 did not incorporate when run in the presence of labeled water. While both of these results have since been discredited—the catalysis is first order in catalyst and is incorporated into... 

Initially, studies on the preparation of the borate complexes of the type 3 using bi-2-naphthol, S-proline and B(OH)3 were carried out. These experiments revealed that the bi-2-naphthol and S-proline form a 2 1 diastereomeric inclusion complex in the absence of boric acid (Scheme l).5 Unfortunately, efforts to improve the optical purity through crystallisation did not yield fruitful results. However, both the enantiomers can be obtained in pure forms by carrying out the experiments again using the partially resolved samples.5... 

Copolymers of L-proline and sarcosine have been prepared by Fasman and Blout (1961). These were found to exist in two forms, analogous to poly-L-proline. Form I, which is obtained directly from the copolymerization mixture showed anomalous optical rotatory dispersion and relatively low viscosity. On dissolving form I in 2-chloroethanol, form II is obtained which exhibits normal optical rotatory dispersion and relatively high viscosity. Fasman and Blout have suggested that the transition, form I —> form II, involves a conversion of the structure from ds- amide bonds to fmns-amide bonds. 

Poly-L-proline, form Acetic acid [m ]M6 +30 NL NL NL (1960) Blout and Fasman... 

Haze formation is mostly attributed to proteins, polyphenols, and their interactions. It is also possible that there are also other factors that inbuence haze formation in beer, but their effect has not been yet clearly debned [ 15]. The amount of haze formed depends both on the concentration of proteins and polyphenols, and on their ratio. Polyphenols can combine with proteins to form colloidal suspensions that scatter light, which creates the cloudy appearance of beer. Beer polyphenols originate partly from barley and partly from hops. The beer polyphenols most closely associated with haze formation are the proanthocyanidins, which are dimers and trimers of catechin, epicatechin, and gaUocatechin. These have been shown to interact strongly with haze-active proteins [13,15-17] and their concentration in beer was directly related to the rate of haze formation [18]. Ahrenst-Larsen and Erdal [19] have demonstrated that anthocyanogen-free barley produces beer that is extremely resistant to haze formation, without any stabilizing treatment, provided that hops do not contribute polyphenols either. Not all proteins are equally involved in haze formation. It has been shown that haze-active proteins contain signibcant amounts of proline and that proteins that lack proline form little or no haze in the presence of polyphenols [13,15-17]. In beer, the source of the haze-active protein has been shown to be the barley hordein, an alcohol-soluble protein rich in proUne [16]. 

Amino acid analysis. There are some 20 amino acids found in proteins and these are released by overnight hydrolysis in 6M HCl. Plasma and urine contain an even larger number of amino acids or related compounds. At low pH, amino acids are cations and for 40 years have been separated by cation exchange column, chromatography. The problem with amino adds is that in general they possess no chromophores by which they can all be detected. In the traditional amino add analyser, their detection was accomplished by a post-column reaction with nin-hydrin which forms a purple colour on heating with an amino acid at pH 5.5. This colour, Ruhemann s purple, is formed with all primary amino acids and can be detected at 570 nm. Secondary amino acids such as proline form a yellow chromophore measurable at 440 nm. 

The side chain of proline forms a ring with the nitrogen attached to the a-carbon. 

Secondary amines and amino acids react in an entirely different way. Indeed, L-proline forms a mixture of the four possible tautomers, but, after a time, ninhydrin-positive substances may be formed by breakdown of the proUne molecule. (Other ketoses do not give this reaction.) Secondary amines, such as piperidine, will not react at 0°, but, at higher temperatures (40-60°), some D-fructosylamine is formed, together with a higher proportion of D-glucose by isomerization. Morpholine or dicyclohexylamine give a 20 to 25% yield of D-n6o-hexulose, and may be used on a preparative... 

What is the major difference between proline and the other amino acids Draw the structure of a dipeptide in which the amino group of proline forms a peptide bond with the carboxyl group of alanine. 

The chemical properties of the polypeptides depend greatly on their complexity. Like amino acids, all the ordinary polypeptides, when their solutions are boiled with precipitated copper oxide, give blue, sometimes blue-violet solutions, and in this way differ from the diketo-piperazines, whose solutions remain colourless, t.e., they do not give copper salts. Leucyl-proline forms again an exception. 

The semi-empirical conformational energy calculations of poly-cis-5-ethylproline (PC5EP) predict that the helical structure may exist in two conformational forms such as I and II. Experimental results confirmed that in solution two major conformations may be assumed by the poly-cis-5-ethyl-D-proline. However, the calculations for poly-trans-5-ethyl-D-proline indicated that only one form may be allowed.Spectroscopic data (Circular Dichroism, NMR) showed the polypeptide exists in a poly-L-proline form-I-type helix and changes slowly to some intermediate conformation. The slow muta-rotation is partially due to the steric interactions of the ethyl group with the carbonyl group of the amide during the mutarotation. 

The stability of poly-L-proline form II helix can be enhanced by decreasing the rotational degree of freedom of the pyrrolidine ring, e.g., poly-3,4-dehydro-L-proline. 

A colloidal suspension of L-proline in dioxane added slowly together with a soln. of phosgene in dioxane to the same solvent, stirred 1 hr. at 45° until a clear soln. results, traces of reactant removed by filtration, degassed in vacuo at 35° for ca. 45 min., the amount of N-chloroformyl-L-proline formed estimated by titration of 1 ml. of the soln. with 0.1 A Ag-nitrate, an equivalent amount of triethylamine added, and stirred 30 min. at room temp. N-carboxy-L-proline anhydride. Y 88%. A. A. Randall, Soc. 1962, 374. 

The Morita-Baylis-Hillman (MBH) reaction is described as the coupling between the a-position of an activated double bond and an sp electrophilic carbon (typically an aldehyde, but also an imine) using an appropriate catalyst, normally Lewis bases [21]. Shi and coworkers showed that imidazole and proline formed an efficient co-catalytic system for carrying out the MBH reaction, but with low ee [22]. 

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