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Related Concept Videos

Calmodulin-dependent Signaling01:16

Calmodulin-dependent Signaling

Calmodulin (CaM) is a calcium-binding protein in eukaryotes that controls various calcium-regulated cellular processes. It has four calcium-binding sites that bind calcium to form the calcium-calmodulin ( Ca2+-CaM) complex. GPCR stimulation increases the calcium levels in the cells that bind to CaM and induces a conformational change.
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
Metal-Semiconductor Junctions01:24

Metal-Semiconductor Junctions

The contact of metal and semiconductor can lead to the formation of a junction with either Schottky or Ohmic behavior.
Schottky Barriers
Schottky barriers arise when a metal with a work function (Φm) contacts a semiconductor with a different work function (Φs). Initially, electrons transfer until the Fermi levels of the metal and semiconductor align at equilibrium. For instance, if Φm > Φs, the semiconductor Fermi level is higher than the metal's before contact. The semiconductor's...
MOSFET: Enhancement Mode01:22

MOSFET: Enhancement Mode

Enhancement-mode MOSFETs are pivotal components in electronics, distinguished by their capacity to act as highly efficient switches. They are part of the larger family of metal-oxide Semiconductor Field-Effect Transistors (MOSFETs). They are available in two types: p-channel and n-channel, each tailored to specific polarity operations.
In their basic form, enhancement-mode MOSFETs are typically non-conductive when the gate-source voltage (Vgs) is zero. This default 'off' state means no current...

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Related Experiment Video

Updated: Jul 6, 2026

Design, Fabrication, and Experimental Characterization of Plasmonic Photoconductive Terahertz Emitters
10:54

Design, Fabrication, and Experimental Characterization of Plasmonic Photoconductive Terahertz Emitters

Published on: July 8, 2013

A calcium-modulated plasmonic switch.

W Paige Hall1, Jeffrey N Anker, Yao Lin

  • 1Department of Chemistry, Northwestern University, 2145 Sheridan Road, Evanston, Illinois 60208, USA.

Journal of the American Chemical Society
|April 12, 2008
PubMed
Summary
This summary is machine-generated.

Researchers developed a novel plasmonic switch using calmodulin to detect protein conformational changes. This localized surface plasmon resonance (LSPR) sensor shows reversible wavelength shifts, enabling real-time analysis of unlabeled protein dynamics.

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07:39

Determination of the Excitation and Coupling Rates Between Light Emitters and Surface Plasmon Polaritons

Published on: July 21, 2018

Area of Science:

  • Biophysics
  • Nanotechnology
  • Spectroscopy

Background:

  • Calmodulin undergoes significant conformational changes upon calcium binding.
  • Localized Surface Plasmon Resonance (LSPR) sensors are sensitive to changes in the local dielectric environment.
  • Developing real-time, label-free methods for monitoring protein dynamics is crucial.

Purpose of the Study:

  • To create a plasmonic switch for detecting calcium-induced calmodulin conformational changes.
  • To utilize LSPR spectroscopy for label-free monitoring of protein dynamics.
  • To develop a high-resolution LSPR spectrometer for sensitive detection of minute wavelength shifts.

Main Methods:

  • Functionalization of an LSPR sensor with a novel calmodulin construct (cutinase-calmodulin-cutinase).
  • Utilizing a high-resolution LSPR spectrometer (1.5 x 10-2 nm resolution) for real-time measurements.
  • Monitoring reversible wavelength modulations (2-3 nm shifts) in response to calcium concentration changes.

Main Results:

  • Demonstrated a reversible wavelength shift of the LSPR extinction maximum (lambdamax) correlating with calcium concentration.
  • Observed a 4-fold faster rate for calmodulin closing (Ca2+-free) compared to opening (Ca2+-bound).
  • Achieved real-time detection of protein conformational dynamics using LSPR without protein labeling.

Conclusions:

  • The developed plasmonic switch effectively detects reversible, calcium-induced conformational changes in calmodulin.
  • LSPR spectroscopy provides a powerful tool for label-free, real-time analysis of unlabeled protein dynamics.
  • This study represents the first application of LSPR spectroscopy for detecting reversible conformational changes in an unlabeled protein.