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Amino stability

The [4+3] cycloaddition between furan and amino-stabilized allyl cations has not been as actively studied. An intramolecular cycloaddition between a furan and a 2-aminoallyl cation, generated from methyleneaziridine under Lewis acid-promoted conditions, is shown in Equation (50) <2004AGE6517>. An AgBF4-promoted asymmetric intermolecular [4+3] cycloaddition of 2-aminoallyl cations, derived from chiral a-chloroimines, with furan to give cycloadducts of up to 60% ee was also reported <1997TL3353>. [Pg.432]

The terf-butylborylene complex 26a,b, which still represents the only example of an alkylborylene complex, displays a significantly different reactivity compared to its amino-stabilized counterpart 23a,b. 26a,b decomposes quickly when it is exposed to air or moisture and a comparable substitution chemistry to that of 23a,b (via 34) cannot be realized. 23a,b proved to be unreactive towards [Pd(PCy3)2]> whereas 26b underwent... [Pg.16]

Thus, pentacarbonylmethoxymethyl-(or phenyl-)carbenechromium, -molybdenum or -tungsten react at RT with diethylaminoethyne or 1-diethylamino-l-propyne to give, in good yields, amino-stabilized carbenes ... [Pg.102]

It is possible to enhance the rate of a Claisen rearrangement, especially in the enolate Claisen reaction. Denmark et al. showed that other carbanionic centers accelerate the Claisen rearrangement (as in Table 11.23).467 Generation of the anion of sulfone 631 (sec. 8.6.A) with various bases led to acceleration of the reaction relative to the thermal reaction of 631 and also influenced the syn/anti ratio (632/633). In general, a donor group at the allyl position accelerates the rate and the presence of an amino stabilizing group increases the rate even more. [Pg.1026]

Figure C2.5.10. The figure gives tire foldability index ct of 27-mer lattice chains witli sets containing different number of amino acids. The sets are generated according to scheme described in [27], The set of 20 amino acids is taken as a standard sample. Each sequence witli 20 amino acids is optimized to fulfil tire stability gap [5]. The residues in tire standard samples are substituted witli four different sets containing a smaller number of amino acids [27]. The foldability of tliese substitutions is indicated by tire full circles. The open diamonds correspond to tire sequences witli same composition. However, tire amino acids are chosen from tire reduced representation and tire resultant sequence is optimized using tire stability gap [5]. Figure C2.5.10. The figure gives tire foldability index ct of 27-mer lattice chains witli sets containing different number of amino acids. The sets are generated according to scheme described in [27], The set of 20 amino acids is taken as a standard sample. Each sequence witli 20 amino acids is optimized to fulfil tire stability gap [5]. The residues in tire standard samples are substituted witli four different sets containing a smaller number of amino acids [27]. The foldability of tliese substitutions is indicated by tire full circles. The open diamonds correspond to tire sequences witli same composition. However, tire amino acids are chosen from tire reduced representation and tire resultant sequence is optimized using tire stability gap [5].
Proteins are biopolymers formed by one or more continuous chains of covalently linked amino acids. Hydrogen bonds between non-adjacent amino acids stabilize the so-called elements of secondary structure, a-helices and / —sheets. A number of secondary structure elements then assemble to form a compact unit with a specific fold, a so-called domain. Experience has shown that a number of folds seem to be preferred, maybe because they are especially suited to perform biological protein function. A complete protein may consist of one or more domains. [Pg.66]

The forces in a protein molecule are modeled by the gradient of the potential energy V(s, x) in dependence on a vector s encoding the amino acid sequence of the molecule and a vector x containing the Cartesian coordinates of all essential atoms of a molecule. In an equilibrium state x, the forces (s, x) vanish, so x is stationary and for stability reasons we must have a local minimizer. The most stable equilibrium state of a molecule is usually the... [Pg.212]

Water-soluble globular proteins usually have an interior composed almost entirely of non polar, hydrophobic amino acids such as phenylalanine, tryptophan, valine and leucine witl polar and charged amino acids such as lysine and arginine located on the surface of thi molecule. This packing of hydrophobic residues is a consequence of the hydrophobic effeci which is the most important factor that contributes to protein stability. The molecula basis for the hydrophobic effect continues to be the subject of some debate but is general considered to be entropic in origin. Moreover, it is the entropy change of the solvent that i... [Pg.531]

NMR signals of the amino acid ligand that are induced by the ring current of the diamine ligand" ". From the temperature dependence of the stability constants of a number of ternary palladium complexes involving dipeptides and aromatic amines, the arene - arene interaction enthalpies and entropies have been determined" ". It turned out that the interaction is generally enthalpy-driven and counteracted by entropy. Yamauchi et al. hold a charge transfer interaction responsible for this effect. [Pg.89]

The fragmentation patterns of 2-acetamido-5-nitrothia2oie (17) and 2-diraethylaminothiazole are reported to be characterized by the stabilization brought by the amino group to the thiazole ring (137). The proposed fragmentation scheme (Scheme 19) displays two major features,... [Pg.28]

The general pattern of alkylation of 2-acylaininothiazoles parallels that of 2-aminothia2ole itself (see Section III.l). In neutral medium attack occurs on the ring nitrogen, and in alkaline medium a mixture of N-ring and N-amino alkylation takes place (40, 43, 161. 163). In acidic medium unusual behavior has been reported (477) 2-acetamido-4-substituted thiazoles react with acetic anhydride in the presence of sulfuric acid to yield 2-acetylimino-3-acetyl-4-phenyl-4-thiazolines (255) when R = Ph. but when R4 = Me or H no acetylation occurs (Scheme 151). The explanation rests perhaps in an acid-catalyzed heterocyclization with an acetylation on the open-chain compound (253), this compound being stabilized... [Pg.91]

Hydrogen bonding stabilizes some protein molecules in helical forms, and disulfide cross-links stabilize some protein molecules in globular forms. We shall consider helical structures in Sec. 1.11 and shall learn more about ellipsoidal globular proteins in the chapters concerned with the solution properties of polymers, especially Chap. 9. Both secondary and tertiary levels of structure are also influenced by the distribution of polar and nonpolar amino acid molecules relative to the aqueous environment of the protein molecules. Nonpolar amino acids are designated in Table 1.3. [Pg.19]

Fig. 3. (a) Chemical stmcture of a synthetic cycHc peptide composed of an alternating sequence of D- and L-amino acids. The side chains of the amino acids have been chosen such that the peripheral functional groups of the dat rings are hydrophobic and allow insertion into Hpid bilayers, (b) Proposed stmcture of a self-assembled transmembrane pore comprised of hydrogen bonded cycHc peptides. The channel is stabilized by hydrogen bonds between the peptide backbones of the individual molecules. These synthetic pores have been demonstrated to form ion channels in Hpid bilayers (71). [Pg.202]

Inactivation and Removal of Viruses. In developing methods of plasma fractionation, the possibiHty of transmitting infection from human vimses present in the starting plasma pool has been recognized (4,5). Consequentiy, studies of product stabiHty encompass investigation of heat treatment of products in both solution (100) and dried (101) states to estabHsh vimcidal procedures that could be appHed to the final product. Salts of fatty acid anions, such as sodium caprylate [1984-06-17, and the acetyl derivative of the amino acid tryptophan, sodium acetyl-tryptophanate [87-32-17, are capable of stabilizing albumin solutions to 60°C for 10 hours (100) this procedure prevents the transmission of viral hepatitis (102,103). The degree of protein stabilization obtained (104) and the safety of the product in clinical practice have been confirmed (105,106). The procedure has also been shown to inactivate the human immunodeficiency vims (HIV) (107). [Pg.530]

The major use of this compound is in the production of mordant and acid dyes. 2-Amino-4-nitropheno1 also has found limited use as an antioxidant and light stabilizer in butyl mbbers and as a catalyst in the manufacture of hexadiene. The compound has been shown to be a skin irritant and continuous exposure should be avoided. Toxicological studies indicate that it is nonaccumulative (162). [Pg.313]


See other pages where Amino stability is mentioned: [Pg.558]    [Pg.168]    [Pg.558]    [Pg.168]    [Pg.2658]    [Pg.48]    [Pg.177]    [Pg.371]    [Pg.87]    [Pg.89]    [Pg.95]    [Pg.100]    [Pg.95]    [Pg.378]    [Pg.82]    [Pg.65]    [Pg.98]    [Pg.191]    [Pg.205]    [Pg.315]    [Pg.532]    [Pg.536]    [Pg.174]    [Pg.202]    [Pg.298]    [Pg.250]    [Pg.277]    [Pg.182]    [Pg.144]    [Pg.396]    [Pg.399]    [Pg.547]    [Pg.242]    [Pg.326]    [Pg.328]    [Pg.359]   
See also in sourсe #XX -- [ Pg.190 ]

See also in sourсe #XX -- [ Pg.280 ]

See also in sourсe #XX -- [ Pg.106 ]




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Amino acids imparting structural stability

Amino acids stability

Amino acids typical stability constants

Amino group, alkyl stabilization

Amino protein stability, composition

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Stability constants amino acid complexes

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Stability with amino acid

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