Frontispiece: Secondary Structure Tuning of a Pseudoprotein Between β‐Meander and α‐Helical Forms in the Solid‐State

Protein Structures In their Research Article (e202113129), Kana M. Sureshan et al. report the secondary structure tuning of a pseudoprotein between β‐meander and α‐helical forms in the solid state.

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Veröffentlicht in:Angewandte Chemie International Edition 2022-01, Vol.61 (4), p.n/a
Hauptverfasser: Athiyarath, Vignesh, Madhusudhanan, Mithun C., Kunnikuruvan, Sooraj, Sureshan, Kana M.
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container_issue 4
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container_title Angewandte Chemie International Edition
container_volume 61
creator Athiyarath, Vignesh
Madhusudhanan, Mithun C.
Kunnikuruvan, Sooraj
Sureshan, Kana M.
description Protein Structures In their Research Article (e202113129), Kana M. Sureshan et al. report the secondary structure tuning of a pseudoprotein between β‐meander and α‐helical forms in the solid state.
doi_str_mv 10.1002/anie.202280462
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source Wiley Online Library - AutoHoldings Journals
subjects azide–alkyne cycloaddition
motion in crystal
Protein structure
pseudoprotein
Secondary structure
topochemical polymerization
Tuning
α-helix
title Frontispiece: Secondary Structure Tuning of a Pseudoprotein Between β‐Meander and α‐Helical Forms in the Solid‐State
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