Tentative Evaluation of the Microdynamics of Tryptophan Residues in Proteins Through Fluorimetric Measurements

Biophysical and Biochemical Information Transfer in Recognition ◽

10.1007/978-1-4899-5330-8_39 ◽

1979 ◽

pp. 451-461

Author(s):

Ivailo V. Zlatanov ◽

Peter P. Chuknyiski ◽

Julia G. Vassileva-Popova

Keyword(s):

Tryptophan Residues

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Amino-acid sequences around methionine and tryptophan residues of hog pepsin

Collection of Czechoslovak Chemical Communications ◽

10.1135/cccc19742709 ◽

1974 ◽

Vol 39 (9) ◽

pp. 2709-2717 ◽

Cited By ~ 1

Author(s):

L. Morávek ◽

V. Kostka

Keyword(s):

Amino Acid ◽

Amino Acid Sequences ◽

Tryptophan Residues

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The amino acid sequence of fragment A, an enzymically active fragment of diphtheria toxin. III. The chymotryptic peptides, the peptides derived by cleavage at tryptophan residues, and the complete sequence of the protein.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)50488-9 ◽

1979 ◽

Vol 254 (13) ◽

pp. 5838-5842

Author(s):

R J DeLange ◽

L C Williams ◽

R E Drazin ◽

R J Collier

Keyword(s):

Amino Acid ◽

Amino Acid Sequence ◽

Diphtheria Toxin ◽

Complete Sequence ◽

Tryptophan Residues ◽

Active Fragment

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Rhodium-Catalyzed C–H Olefination of Tryptophan Residues

Synfacts ◽

10.1055/s-0040-1706083 ◽

2020 ◽

Vol 17 (01) ◽

pp. 0104

Keyword(s):

Tryptophan Residues

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The rates of photodestruction of tryptophan residues in human and bovine ocular lens proteins

Experimental Eye Research ◽

10.1016/0014-4835(81)90024-5 ◽

1981 ◽

Vol 32 (6) ◽

pp. 747-754 ◽

Cited By ~ 27

Author(s):

R.F Borkman ◽

J.D Tassin ◽

S Lerman

Keyword(s):

Ocular Lens ◽

Lens Proteins ◽

Tryptophan Residues

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Close proximity of tryptophan residues and ATP-binding site in Escherichia coli primary replicative helicase DnaB protein. Molecular topography of the enzyme.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)31702-2 ◽

1994 ◽

Vol 269 (50) ◽

pp. 31359-31371 ◽

Cited By ~ 1

Author(s):

W Bujalowski ◽

M M Klonowska

Keyword(s):

Escherichia Coli ◽

Binding Site ◽

Atp Binding ◽

Replicative Helicase ◽

Atp Binding Site ◽

Close Proximity ◽

Tryptophan Residues ◽

Helicase Dnab

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Engineered Tet repressor mutants with single tryptophan residues as fluorescent probes. Solvent accessibilities of DNA and inducer binding sites and interaction with tetracycline.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)47899-4 ◽

1987 ◽

Vol 262 (29) ◽

pp. 14030-14035

Author(s):

D Hansen ◽

L Altschmied ◽

W Hillen

Keyword(s):

Fluorescent Probes ◽

Binding Sites ◽

Tryptophan Residues ◽

Tet Repressor

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Analysis of the role of tryptophan residues in the Flourescence of the maltose-binding protein according to a simple model

Journal of Molecular Biology ◽

10.1016/0022-2836(90)90166-j ◽

1990 ◽

Vol 214 (1) ◽

pp. 350-352

Author(s):

Pierre Martineau

Keyword(s):

Simple Model ◽

Binding Protein ◽

Maltose Binding Protein ◽

Tryptophan Residues

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On the effects of replacing the carboxylate-binding arginine-171 by hydrophobic tyrosine or tryptophan residues in the L-lactate dehydrogenase from Bacillus stearothermophilus

Biochemistry ◽

10.1021/bi00442a011 ◽

1989 ◽

Vol 28 (16) ◽

pp. 6605-6610 ◽

Cited By ~ 10

Author(s):

Marcel A. Luyten ◽

Marvin Gold ◽

James D. Friesen ◽

J. Bryan Jones

Keyword(s):

Lactate Dehydrogenase ◽

Bacillus Stearothermophilus ◽

Tryptophan Residues

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Role of Tryptophan Residues in Gramicidin Channel Organization and Function

Biophysical Journal ◽

10.1529/biophysj.107.124206 ◽

2008 ◽

Vol 95 (1) ◽

pp. 166-175 ◽

Cited By ~ 29

Author(s):

Amitabha Chattopadhyay ◽

Satinder S. Rawat ◽

Denise V. Greathouse ◽

Devaki A. Kelkar ◽

Roger E. Koeppe

Keyword(s):

Gramicidin Channel ◽

Tryptophan Residues ◽

And Function

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The Effects of Biological Environments on the Electron-Relay Functionality of Tryptophan Residues in Proteins

ChemPhysChem ◽

10.1002/cphc.201100713 ◽

2011 ◽

Vol 13 (1) ◽

pp. 183-192 ◽

Cited By ~ 3

Author(s):

Xiaohua Chen ◽

Hongjing Dai ◽

Jilai Li ◽

Xuri Huang ◽

Zidong Wei

Keyword(s):

Tryptophan Residues

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