Photomodulation of conformational states. III. Water-soluble bis-cysteinyl-peptides with (4-aminomethyl) phenylazobenzoic acid as backbone constituent. (Q30683116)

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English	Photomodulation of conformational states. III. Water-soluble bis-cysteinyl-peptides with (4-aminomethyl) phenylazobenzoic acid as backbone constituent.	scientific article

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8 December 2019

Photomodulation of conformational states. III. Water-soluble bis-cysteinyl-peptides with (4-aminomethyl) phenylazobenzoic acid as backbone constituent (English)

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8 December 2019

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8 December 2019

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Christian Renner

1

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8 December 2019

Raymond Behrendt

2

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8 December 2019

Nicola Heim

3

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8 December 2019

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1 May 2002

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8 December 2019

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8 December 2019

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8 December 2019

6

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8 December 2019

382-393

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8 December 2019

Photoresponsive cyclic bis(cysteinyl)peptides as catalysts of oxidative protein folding.

1 reference

https://api.crossref.org/works/10.1002%2FBIP.10127

21 January 2018

Photo-control of helix content in a short peptide

1 reference

https://api.crossref.org/works/10.1002%2FBIP.10127

21 January 2018

Convergent evolution of similar function in two structurally divergent enzymes

1 reference

https://api.crossref.org/works/10.1002%2FBIP.10127

21 January 2018

Determination of three-dimensional structures of proteins from interproton distance data by dynamical simulated annealing from a random array of atoms. Circumventing problems associated with folding

1 reference

https://api.crossref.org/works/10.1002%2FBIP.10127

21 January 2018

Thioredoxin--a fold for all reasons

1 reference

https://api.crossref.org/works/10.1002%2FBIP.10127

21 January 2018

Structure determination of the N-terminal thioredoxin-like domain of protein disulfide isomerase using multidimensional heteronuclear 13C/15N NMR spectroscopy

1 reference

https://api.crossref.org/works/10.1002%2FBIP.10127

21 January 2018

Why is DsbA such an oxidizing disulfide catalyst?

1 reference

https://api.crossref.org/works/10.1002%2FBIP.10127

21 January 2018

Elimination of all charged residues in the vicinity of the active-site helix of the disulfide oxidoreductase DsbA. Influence of electrostatic interactions on stability and redox properties.

1 reference

https://api.crossref.org/works/10.1002%2FBIP.10127

21 January 2018

Influence of acidic residues and the kink in the active-site helix on the properties of the disulfide oxidoreductase DsbA.

1 reference

https://api.crossref.org/works/10.1002%2FBIP.10127

21 January 2018

Peptide oligomers for holographic data storage

1 reference

https://api.crossref.org/works/10.1002%2FBIP.10127

21 January 2018

Photoswitchable Hydrogen-Bonding in Self-Organized Cylindrical Peptide Systems

1 reference

https://api.crossref.org/works/10.1002%2FBIP.10127

21 January 2018

Photomodulation of the Conformation of Cyclic Peptides with Azobenzene Moieties in the Peptide Backbone

1 reference

https://api.crossref.org/works/10.1002%2FBIP.10127

21 January 2018

Photomodulation of conformational states. Synthesis of cyclic peptides with backbone-azobenzene moieties

1 reference

https://api.crossref.org/works/10.1002%2FBIP.10127

21 January 2018

Photomodulation of conformational states. I. Mono- and bicyclic peptides with (4-amino)phenylazobenzoic acid as backbone constituent

1 reference

https://api.crossref.org/works/10.1002%2FBIP.10127

21 January 2018

Photomodulation of conformational states. II. Mono- and bicyclic peptides with (4-aminomethyl)phenylazobenzoic acid as backbone constituent

1 reference

https://api.crossref.org/works/10.1002%2FBIP.10127

21 January 2018

Redox-active bis-cysteinyl peptides. I. Synthesis of cyclic cystinyl peptides by conventional methods in solution and on solid supports

1 reference

https://api.crossref.org/works/10.1002%2FBIP.10127

21 January 2018

47. Crystal structure and configuration of the isomeric azobenzenes

1 reference

https://api.crossref.org/works/10.1002%2FBIP.10127

21 January 2018

A single dipeptide sequence modulates the redox properties of a whole enzyme family

1 reference

https://api.crossref.org/works/10.1002%2FBIP.10127

21 January 2018

Conserved residues flanking the thiol/disulfide centers of protein disulfide isomerase are not essential for catalysis of thiol/disulfide exchange

1 reference

https://api.crossref.org/works/10.1002%2FBIP.10127

21 January 2018

Redox-active bis-cysteinyl peptides. II. Comparative study on the sequence-dependent tendency for disulfide loop formation

1 reference

https://api.crossref.org/works/10.1002%2FBIP.10127

21 January 2018

Redox potentials of active-site bis(cysteinyl) fragments of thiol-protein oxidoreductases

1 reference

https://api.crossref.org/works/10.1002%2FBIP.10127

21 January 2018

Identifiers

10.1002/BIP.10127

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Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11920439%20AND%20SRC:MED&resulttype=core&format=json

8 December 2019

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11920439%20AND%20SRC:MED&resulttype=core&format=json

8 December 2019

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