Optical Rotation of Peptides. IV. Lysine Tripeptides<sup>1</sup>

Brand, Erwin; Erlanger, Bernard F.; Polatnick, Jerome; Sachs, Hans; Kirschenbaum, Donald M.

doi:10.1021/ja01152a520

Cited by 18 publications

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“…As corrcctly pointed out by Schechter and Berger (22), although the Brand and co-workers treatment (18,19) describes the situation fairly well, it clearly represents an oversiniplification of the problem. In fact, it introduces an artificial concept, namely a residue optical activity as an additive parameter assigned to an asymmetric carbon atom.…”

Section: Resultsmentioning

confidence: 90%

“…They also made the first systematic study of D-line rotations of various series of oligopeptides (19). Later on, Tanford and coworkers were able to demonstrate that the amino acid composition affects the ord properties from unordered regions of protein chains (20).…”

Section: Resultsmentioning

confidence: 99%

“…Later on, Tanford and coworkers were able to demonstrate that the amino acid composition affects the ord properties from unordered regions of protein chains (20). The approach of Brand and co-workers (18,19) (23).…”

Section: Resultsmentioning

confidence: 99%

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Linear oligopeptides. XXVII. Contribution to the circular dichroism of internal peptide chromophores

Toniolo¹,

Bonora²

1976

Can. J. Chem.

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-l~cxall~1oropro~~a1~-2-ol were calci~lated by subtracting the total molar ellipticity values of N-and C-protected homo-trimers from those of the pertinent protected homo-tetramers.The circular dichroism of the internal peptide chromophore of aliphatic hydrocarbon-and s~llfur-containing peptides, each of the L-configuration, show a negative band at 21 5-230 nm accompanied by a more intense negative band near 200 nm. A structi~red wcak and negative band near 260 nm along with bands at 240 nm (negative), 222 nm (positive), and 210.5 nm (negative) of progressively increasing intensity are apparent in the circular dichroic spectrilln of L-Phe-L-Phe internal peptide chro~nophore. The elfect of solvent polarity is discilssed in thc case of L-Val-L-Val and L-Ala-L-Ala internal peptide chromophores.Among the protected ho~no-trimers and tetramers only those of L-alanine are soluble in aqileoils solution; consequently, the effect of water as a function of temperature, urea, and guanidinium chloride on the L-Ala-L-Ala internal peptide chromophore circular dichroism was established.CLAUDIO TONIOLO et GIAN MARIA BONORA. Can. J. Chem. 5'470 (1976). On a calci~le la contribution des chro~nophores peptidiques internes ail dichroismc circillaire Parmi les homo trimkres et tetramkres protCgCs seulement cells de la L-alaninc sont solubles dans des solutions aqueuses; par consCquent I'effet dc I'ea~i cn fonction de la temperature,

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Section: Resultsmentioning

confidence: 90%

Section: Resultsmentioning

confidence: 99%

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Linear oligopeptides. XXVII. Contribution to the circular dichroism of internal peptide chromophores

Toniolo¹,

Bonora²

1976

Can. J. Chem.

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“…Previous preparations of peptides containing Z ε ‐lysine utilized coupling reagents‐like carbodiimides (3–7,10,12–18) and BOP (9). Peptide coupling has also been achieved using the mixed anhydride method (8,11,19–22), the azide method (23–25), the active ester method (formyl‐substituted nitrophenylthio esters; 26). However, all these methodologies require long reaction times (18–24 h).…”

mentioning

confidence: 99%

“…For example, the coupling of N‐protected amino acid with Z ε ‐lysine or its corresponding ester in the presence of DCC/HOBT requires 18–24 h to achieve completion (3,4,8,10,11,13,17–19,26). In some cases, the final product is an ester and thus requires hydrolysis or hydrogenolysis as an additional step to obtain the desired free peptide (3,4,10,11,19,21,23–25).…”

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confidence: 99%