The Influence of Two-Dimensional Organization on Peptide Conformation

Simon White; Steven David Johnson; Mark Sellick; Agnieszka Bronowska; Peter Stockley; Christoph Walti

doi:10.1002/anie.201408971

The Influence of Two-Dimensional Organization on Peptide Conformation

Simon White, Steven David Johnson, Mark Sellick, Agnieszka Bronowska, Peter Stockley, Christoph Walti

Electronic Engineering

Research output: Contribution to journal › Article › peer-review

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.

Original language	English
Pages (from-to)	974-978
Number of pages	5
Journal	Angewandte chemie-International edition
Volume	54
Issue number	3
DOIs	https://doi.org/10.1002/anie.201408971
Publication status	Published - 12 Jan 2015

Keywords

COILED COILS
MOLECULAR CROWDING
CIRCULAR DICHROISM

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10.1002/anie.201408971

Steven David Johnson
- steven.johnsonyork.acuk
- Electronic Engineering - Professor
Person: Academic

C2D2 research 1b - Point-of-care, electronic detection of pathogenic bacteria using redox-active biomarkers
Johnson, S. D. & Moir, J.
1/07/12 → 31/03/13
Project: Other project › Other internal award

Cite this

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title = "The Influence of Two-Dimensional Organization on Peptide Conformation",

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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AU - Johnson, Steven David

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AU - Bronowska, Agnieszka

AU - Stockley, Peter

AU - Walti, Christoph

PY - 2015/1/12

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N2 - 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.

AB - 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.

KW - COILED COILS

KW - MOLECULAR CROWDING

KW - CIRCULAR DICHROISM

U2 - 10.1002/anie.201408971

DO - 10.1002/anie.201408971

M3 - Article

SN - 1433-7851

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JO - Angewandte chemie-International edition

JF - Angewandte chemie-International edition

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ER -

The Influence of Two-Dimensional Organization on Peptide Conformation

Abstract

Keywords

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Profiles

Steven David Johnson

Projects

C2D2 research 1b - Point-of-care, electronic detection of pathogenic bacteria using redox-active biomarkers

Cite this