ArticleAngewandte Chemie (International ed. in English)2015
The influence of two-dimensional organization on peptide conformation.
Article in Angewandte Chemie (International ed. in English), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
9 citing papers in PubMed.
- Electronic Actuation of Surface-Immobilized, pH-Responsive DNA Nanoswitches.ACS applied materials & interfaces · 2026Article
- Chemical and Enzymatic Synthesis of Sialylated Glycoforms of Human Erythropoietin.Angewandte Chemie (International ed. in English) · 2021Article
- Direct Immobilization of Engineered Nanobodies on Gold Sensors.ACS applied materials & interfaces · 2021Article
- Probing Protein Folding with Sequence-Reversed α-Helical Bundles.International journal of molecular sciences · 2021Article
- One Peptide for Them All: Gold Nanoparticles of Different Sizes Are Stabilized by a Common Peptide Amphiphile.ACS nano · 2020Article
- Chiroptical Sensing: A Conceptual Introduction.Sensors (Basel, Switzerland) · 2020Review
- Experimental characterization and simulation of amino acid and peptide interactions with inorganic materials.Engineering in life sciences · 2018Review
- Electric fields control the orientation of peptides irreversibly immobilized on radical-functionalized surfaces.Nature communications · 2018Article
- Investigating the dynamics of surface-immobilized DNA nanomachines.Scientific reports · 2016Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
Molecular crowding plays a significant role in regulating molecular conformation in cellular environments. It is also likely to be important wherever high molecular densities are required, for example in surface-phase studies, in which molecular densities generally far exceed those observed in solution. Using on-surface circular dichroism (CD) spectroscopy, we have investigated the structure of a synthetic peptide assembled into a highly packed monolayer. The immobilized peptide undergoes a structural transition between α-helical and random coil conformation upon changes in pH and ionic concentration, but critically the threshold for conformational change is altered dramatically by molecular crowding within the peptide monolayer. This study highlights the often overlooked role molecular crowding plays in regulating molecular structure and function in surface-phase studies of biological molecules.
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Registered trials
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