Membrane Organization and Dynamics of “Inner Pair” and “Outer Pair” Tryptophan Residues in Gramicidin Channels

The Journal of Physical Chemistry B ◽

10.1021/jp304846f ◽

2012 ◽

Vol 116 (36) ◽

pp. 11056-11064 ◽

Author(s):

Sourav Haldar ◽

Arunima Chaudhuri ◽

Hong Gu ◽

Roger E. Koeppe ◽

Mamata Kombrabail ◽

...

Keyword(s):

Membrane Organization ◽

Tryptophan Residues ◽

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Faculty Opinions recommendation of Eisosome-driven plasma membrane organization is mediated by BAR domains.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.12005957.13135055 ◽

2011 ◽

Author(s):

Mark Rose

Keyword(s):

Plasma Membrane ◽

Membrane Organization ◽

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Faculty Opinions recommendation of Diffusion analysis within single nanometric apertures reveals the ultrafine cell membrane organization.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.723477950.793511406 ◽

2015 ◽

Author(s):

Satyajit Mayor

Keyword(s):

Cell Membrane ◽

Membrane Organization ◽

Diffusion Analysis

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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 ◽

Author(s):

L. Morávek ◽

V. Kostka

Keyword(s):

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 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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Eisosomes and plasma membrane organization

Molecular Genetics and Genomics ◽

10.1007/s00438-012-0706-8 ◽

2012 ◽

Vol 287 (8) ◽

pp. 607-620 ◽

Author(s):

Agustina Olivera-Couto ◽

Pablo S. Aguilar

Keyword(s):

Plasma Membrane ◽

Membrane Organization

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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 ◽

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 ◽

Author(s):

W Bujalowski ◽

M M Klonowska

Keyword(s):

Escherichia Coli ◽

Binding Site ◽

Atp Binding ◽

Replicative Helicase ◽

Atp Binding Site ◽

Close Proximity ◽

Tryptophan Residues ◽

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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 ◽

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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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