Observations on the reaction of 2-hydroxy-5-nitrobenzyl bromide with a peptide-bound tryptophanyl residue

1984 ◽  
Vol 136 (1) ◽  
pp. 93-100 ◽  
Author(s):  
Roger L. Lundblad ◽  
Claudia M. Noyes
Keyword(s):  
Tryptophanyl Residue

Intramembrane position of the fluorescent tryptophanyl residue in membrane-bound cytochrome b5

Biochemistry ◽  
1979 ◽  
Vol 18 (24) ◽  
pp. 5458-5464 ◽  
Author(s):  
Patrick J. Fleming ◽  
Dennis E. Koppel ◽  
Arthur L. Y. Lau ◽  
Philipp Strittmatter
Keyword(s):  
Cytochrome B5 ◽  
Membrane Bound ◽  
Tryptophanyl Residue

Involvement and identification of a tryptophanyl residue at the pyruvate binding site of transcarboxylase

Biochemistry ◽  
1988 ◽  
Vol 27 (16) ◽  
pp. 5978-5983 ◽  
Author(s):  
Ganesh K. Kumar ◽  
F. Carl Haase ◽  
Nelson F. B. Phillips ◽  
Harland G. Wood
Keyword(s):  
Binding Site ◽  
Tryptophanyl Residue

CONFORMATIONAL STUDIES ON SYNTHETIC POLY-α-AMINO ACIDS: THE HELICAL SENSE OF POLY-L-TRYPTOPHAN: OPTICAL ROTATORY DISPERSION STUDIES

1965 ◽  
Vol 43 (5) ◽  
pp. 1588-1598 ◽  
Author(s):  
Gerald D. Fasman ◽  
Margarete Landsberg ◽  
Manuel Buchwald
Keyword(s):  
Wavelength Range ◽  
Cotton Effect ◽  
Optical Rotatory Dispersion ◽  
Rotatory Dispersion ◽  
Helical Conformation ◽  
Optical Rotatory ◽  
Negative Cotton Effect ◽  
Cotton Effects ◽  
The Right ◽  
Tryptophanyl Residue

The synthesis of high molecular weight (100 000 to 200 000) polymers and copolymers of L-tryptophan and γ-benzyl-L-glutamate is reported. The optical rotatory dispersion (o.r.d.) of these polypeptides is recorded in the wavelength range 540–320 mμ and the b0 values of the Moffitt equation, using λ0 = 212ν, are listed. Poly-L-tryptophan has a b0 value of +570 in dimethylformamide (DMF). A linear relationship exists between this value, b0 values of copolymers of various ratios of L-tryptophan and γ-benzyl-L-glutamate, and the value of− 670 found for poly-γ-benzyl-L-glutamate. The o.r.d. curve of a poly-L-tryptophan film, in the 330–200 mμ wavelength range, reveals two positive Cotton effects in the 270–290 mμ region and a large negative Cotton effect at 233 mμ. Thus, despite the positive b0 value, these data prove that poly-L-tryptophan, in DMF, has the right-handed helical conformation. Hypochromicity was found for the tryptophanyl residue in the helical polypeptide. The rotatory contribution of chromophores, such as tryptophan or coenzymes, when bound asymmetrically to a protein, can be very significant, and caution is advised in the interpretation of such o.r.d. curves.

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