Probing the ligand-binding specificity and analyzing the folding state of SPOT-synthesized FBP28 WW domain variants. (Q52933821)

9 May 2018

title

Probing the ligand-binding specificity and analyzing the folding state of SPOT-synthesized FBP28 WW domain variants. (English)

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9 May 2018

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Jana Przezdziak

1

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9 May 2018

Sandra Tremmel

2

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9 May 2018

Ines Kretzschmar

3

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9 May 2018

Michael Beyermann

4

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9 May 2018

Michael Bienert

5

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9 May 2018

Rudolf Volkmer-Engert

6

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9 May 2018

publication date

1 May 2006

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9 May 2018

published in

ChemBioChem

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9 May 2018

volume

7

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9 May 2018

issue

5

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9 May 2018

page(s)

780-788

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9 May 2018

WW domain sequence activity relationships identified using ligand recognition propensities of 42 WW domains

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WW: An isolated three-stranded antiparallel beta-sheet domain that unfolds and refolds reversibly; evidence for a structured hydrophobic cluster in urea and GdnHCl and a disordered thermal unfolded state

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Incorporating beta-turns and a turn mimetic out of context in loop 1 of the WW domain affords cooperatively folded beta-sheets

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21 January 2018

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Solution structures of the YAP65 WW domain and the variant L30 K in complex with the peptides GTPPPPYTVG, N-(n-octyl)-GPPPY and PLPPY and the application of peptide libraries reveal a minimal binding epitope

21 January 2018

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Identifiers

DOI

10.1002/CBIC.200500408

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9 May 2018

1 reference

9 May 2018