Tryptophan-based fluorophores for studying protein conformational changes. - Wikidata - awgldk - TriplyDB

Tryptophan-based fluorophores for studying protein conformational changes.

Tryptophan-based fluorophores for studying protein conformational changes.

http://www.wikidata.org/entity/Q34623999

about

Bioconjugation of therapeutic proteins and enzymes using the expanded set of genetically encoded amino acids.Comparison of biological chromophores: photophysical properties of cyanophenylalanine derivatives.Synthesis and Evaluation of a Library of Fluorescent Dipeptidomimetic Analogues as Substrates for Modified Bacterial Ribosomes.Recent advances in the synthesis and application of fluorescent α-amino acids.Blue fluorescent amino acid for biological spectroscopy and microscopy.Toward intrinsically colored peptides: Synthesis and investigation of the spectral properties of methylated azatryptophans in tryptophan-cage mutants.

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P2860

Tryptophan-based fluorophores for studying protein conformational changes.

http://www.wikidata.org/entity/Q34623999

description

2014 nî lūn-bûn

@nan

2014 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2014 թվականի սեպտեմբերին հրատարակված գիտական հոդված

@hy

2014年の論文

@ja

2014年論文

@yue

2014年論文

@zh-hant

2014年論文

@zh-hk

2014年論文

@zh-mo

2014年論文

@zh-tw

2014年论文

@wuu

name

Tryptophan-based fluorophores for studying protein conformational changes.

@ast

Tryptophan-based fluorophores for studying protein conformational changes.

@en

Tryptophan-based fluorophores for studying protein conformational changes.

@nl

type

label

Tryptophan-based fluorophores for studying protein conformational changes.

@ast

Tryptophan-based fluorophores for studying protein conformational changes.

@en

Tryptophan-based fluorophores for studying protein conformational changes.

@nl

prefLabel

Tryptophan-based fluorophores for studying protein conformational changes.

@ast

Tryptophan-based fluorophores for studying protein conformational changes.

@en

Tryptophan-based fluorophores for studying protein conformational changes.

@nl

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J.BMC.2014.09.015

P1433

Bioorganic & Medicinal Chemistry

P1476

Tryptophan-based fluorophores for studying protein conformational changes.

@en

P2093

C Tony Liu

http://www.w3.org/2001/XMLSchema#string

Edwin A Baldwin

http://www.w3.org/2001/XMLSchema#string

Poulami Talukder

http://www.w3.org/2001/XMLSchema#string

Shengxi Chen

http://www.w3.org/2001/XMLSchema#string

Sidney M Hecht

http://www.w3.org/2001/XMLSchema#string

Stephen J Benkovic

http://www.w3.org/2001/XMLSchema#string

P2860

Mechanisms of tryptophan fluorescence shifts in proteins

A dynamic knockout reveals that conformational fluctuations influence the chemical step of enzyme catalysis

Crystal structures of Escherichia coli dihydrofolate reductase: the NADP+ holoenzyme and the folate.NADP+ ternary complex. Substrate binding and a model for the transition state

Crystal structures of Escherichia coli and Lactobacillus casei dihydrofolate reductase refined at 1.7 A resolution. I. General features and binding of methotrexate

Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: crystallographic evidence

The green fluorescent protein

Fluorescent indicators for Ca2+ based on green fluorescent proteins and calmodulin

Spectroscopic determination of tryptophan and tyrosine in proteins

Fluorescence resonance energy transfer between unnatural amino acids in a structurally modified dihydrofolate reductase.

Fluorescent biphenyl derivatives of phenylalanine suitable for protein modification.

P304

5924-5934

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scholarly article

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10.1016/J.BMC.2014.09.015

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21

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4254292

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