Chemical Modification of the Tryptophan Residue in a Recombinant Ca2+-ATPase N-domain for Studying Tryptophan-ANS FRET

10.3791/62770 ◽  
2021 ◽  
Author(s):  
José G. Sampedro ◽  
Yolanda Cataño
Keyword(s):  
Chemical Modification ◽  
Tryptophan Residue

Chemical modification of the tryptophan residue in toxin B from the venom of the Indian cobra

1974 ◽  
Vol 57 (4) ◽  
pp. 973-979 ◽  
Author(s):  
Mitsuhiro Ohta ◽  
Kyozo Hayashi
Keyword(s):  
Chemical Modification ◽  
Tryptophan Residue ◽  
Toxin B

Effect Of pH On The Stability And Conformation Of α-Thrombin

1981 ◽  
Author(s):  
German B Villanueva
Keyword(s):  
Chemical Modification ◽  
Structural Changes ◽  
Low Ph ◽  
Tryptophan Residue ◽  
Difference Spectroscopy ◽  
Compact Structure ◽  
Tyrosine Residues ◽  
Charge Interaction ◽  
The Stability ◽  
Peptide Region

It is known that storage at pH 6 stabilizes thrombin against inactivation. In order to determine whether structural changes accompany this stabilization, the conformation of human α-thrombin at pH 6.0 and 7.5 was investigated by chemical modification, solvent perturbation, UV difference spectroscopy and circular dichroism. It was shown that the CD spectra of α-thrombin at 230-200 nm peptide region were indistinguishable at two pH values indicating no difference in the secondary structure. However, differences were observed in the 320-250 nm aromatic region suggesting some changes in the microenvironment of the aromatic chromophores. Solvent perturbation in 20% ethylene glycol indicated 3.7 ± 0.5 Trp and 7.8 ± 0.5 Tyr were exposed to the solvent at pH 6.0 while 4.3 ± 0.4 Trp and 8.4 ± 0.5 Tyr were exposed at pH 7.5. Chemical modification of tryptophan residue by dimethyl(2-hydroxy- 5-nitrobenzyl)sulfonium bromide in a 100-fold molar excess of the reagent showed 3 reactive residues at pH 6.0 and 6 at pH 7.5. These results suggest that when thrombin is exposed to low pH, structural changes occur that decrease the relative degree of exposure of tryptophan and tyrosine residues. Furthermore, UV difference spectroscopy showed the development of a positive differential spectrum when thrombin at pH 6.0 was exposed to pH 7.5. From this study, it is concluded that the stability of thrombin at pH 6.0 is due to a more compact structure of the enzyme which is probably a result of reduced charge interaction at low pH.

Chemical modification of dipeptidyl peptidase IV: Involvement of an essential tryptophan residue at the substrate binding site

1984 ◽  
Vol 234 (2) ◽  
pp. 622-628 ◽  
Author(s):  
Minoru Harada ◽  
B.Yukihiro Hiraoka ◽  
Kayoko M. Fukasawa ◽  
Katsuhiko Fukasawa
Keyword(s):  
Chemical Modification ◽  
Binding Site ◽  
Substrate Binding ◽  
Dipeptidyl Peptidase ◽  
Dipeptidyl Peptidase Iv ◽  
Tryptophan Residue ◽  
Substrate Binding Site

A reversible chemical modification of the tryptophan residue

1967 ◽  
Vol 147 (3) ◽  
pp. 453-461 ◽  
Author(s):  
Aldo Previero ◽  
Maria Antonia Coletti-Previero ◽  
Jean-Claude Cavadore
Keyword(s):  
Chemical Modification ◽  
Tryptophan Residue

An active center tryptophan residue in dihydrofolate reductase: Chemical modification, sequence surrounding the critical residue, and structural homology considerations

1977 ◽  
Vol 180 (2) ◽  
pp. 310-317 ◽  
Author(s):  
James H. Freisheim ◽  
Lowell H. Ericsson ◽  
Kamal G. Bitar ◽  
R.Bruce Dunlap ◽  
Anthony V. Reddy
Keyword(s):  
Chemical Modification ◽  
Active Center ◽  
Dihydrofolate Reductase ◽  
Tryptophan Residue ◽  
Structural Homology ◽  
Critical Residue

scholarly journals Evidence by chemical modification that tryptophan-104 of the cysteine-proteinase inhibitor chicken cystatin is located in or near the proteinase-binding site

1990 ◽  
Vol 271 (1) ◽  
pp. 281-284 ◽  
Author(s):  
M Nycander ◽  
I Björk
Keyword(s):  
Absorption Spectrum ◽  
Chemical Modification ◽  
Binding Site ◽  
Proteinase Inhibitor ◽  
Cysteine Proteinase ◽  
Dissociation Rate ◽  
Tryptophan Residue ◽  
Cysteine Proteinase Inhibitor ◽  
Lower Affinity ◽  
Chicken Cystatin

The single tryptophan residue Trp-104 of chicken cystatin was modified with a 2-hydroxy-5-nitrobenzyl group. The change of the absorption spectrum of this group on binding of the modified cystatin to papain indicated a decreased environmental polarity of the probe. The modified inhibitor had about a 10(5)-fold lower affinity for papain than had intact cystatin, this being due to a higher dissociation rate constant. These results show that Trp-104 of cystatin is located in or near the proteinase-binding site of the inhibitor, in agreement with a model proposed from computer docking Experiments.

Chemical modification of the tryptophan residue in adrenocorticotropin

Biochemistry ◽  
1976 ◽  
Vol 15 (4) ◽  
pp. 921-927 ◽  
Author(s):  
Eleanor Canova-Davis ◽  
J. Ramachandran
Keyword(s):  
Chemical Modification ◽  
Tryptophan Residue

Chemical modification of the tryptophan residue in cobratoxin

1969 ◽  
Vol 37 (5) ◽  
pp. 841-846 ◽  
Author(s):  
C.C. Chang ◽  
K. Hayashi
Keyword(s):  
Chemical Modification ◽  
Tryptophan Residue

Photoconductivity in Vacuum Deposited Films of Silicon-Based Polymers

1996 ◽  
Vol 444 ◽  
Author(s):  
H. Okumoto ◽  
M. Shimomura ◽  
N. Minami ◽  
Y. Tanabe
Keyword(s):  
Charge Transfer ◽  
Chemical Modification ◽  
Electronic Transport ◽  
Hole Transport ◽  
Electron Acceptors ◽  
Oxygen Atmosphere ◽  
Dangling Bonds ◽  
Silicon Based ◽  
Deposited Films

AbstractSilicon-based polymers with σconjugated electrons have specific properties; photoreactivity for microlithography and photoconductivity for hole transport materials. To explore the possibility of combining these two properties to develop photoresists with electronic transport capability, photoconductivity of polysilanes is investigated in connection with their photoinduced chemical modification. Increase in photocurrent is observed accompanying photoreaction of poly(dimethylsilane) vacuum deposited films. This increase is found to be greatly enhanced in oxygen atmosphere. Such changes of photocurrent can be explained by charge transfer to electron acceptors from Si dangling bonds postulated to be formed during photoreaction.

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