Spectroscopic Monitoring of Mechanical Forces during Protein Folding by using Molecular Force Probes

ChemPhysChem ◽  
2016 ◽  
Vol 17 (10) ◽  
pp. 1486-1492 ◽  
Author(s):  
Tim Stauch ◽  
Marvin T. Hoffmann ◽  
Andreas Dreuw
Keyword(s):  
Protein Folding ◽  
Mechanical Forces ◽  
Spectroscopic Monitoring ◽  
Molecular Force ◽  
Force Probes

Biological Force Measurements Using Micromachined Cantilevers

1999 ◽  
Author(s):  
Y. Liang ◽  
J. N. Welch ◽  
R. G. Rudnitsky ◽  
T. W. Kenny
Keyword(s):  
Protein Folding ◽  
Receptor Binding ◽  
Biological Systems ◽  
Cellular Adhesion ◽  
Measuring Instruments ◽  
Mechanical Forces ◽  
Force Measurements ◽  
Work In Progress ◽  
Micromechanical Force

Abstract There are many interesting biological systems that utilize small mechanical forces to achieve functionality. Protein folding, ligand-receptor binding, cellular adhesion, and others all rely on picoNewton sized mechanical forces. In many of these examples, the fundamental character of the interaction remains controversial. In this paper, we describe work in progress to develop micromechanical force-measuring instruments suitable for measurements of these small biologically derived forces.

Molecular Force Measurement with Tension Sensors

2021 ◽  
Vol 50 (1) ◽  
Author(s):  
Lisa S. Fischer ◽  
Srishti Rangarajan ◽  
Tanmay Sadhanasatish ◽  
Carsten Grashoff
Keyword(s):  
Molecular Mechanisms ◽  
Force Measurement ◽  
Annual Review ◽  
Publication Date ◽  
Mechanical Forces ◽  
Biophysical Parameters ◽  
Cellular Mechanotransduction ◽  
Molecular Force ◽  
Molecular Forces ◽  
Physical Principles

The ability of cells to generate mechanical forces, but also to sense, adapt to, and respond to mechanical signals, is crucial for many developmental, postnatal homeostatic, and pathophysiological processes. However, the molecular mechanisms underlying cellular mechanotransduction have remained elusive for many decades, as techniques to visualize and quantify molecular forces across individual proteins in cells were missing. The development of genetically encoded molecular tension sensors now allows the quantification of piconewton-scale forces that act upon distinct molecules in living cells and even whole organisms. In this review, we discuss the physical principles, advantages, and limitations of this increasingly popular method. By highlighting current examples from the literature, we demonstrate how molecular tension sensors can be utilized to obtain access to previously unappreciated biophysical parameters that define the propagation of mechanical forces on molecular scales. We discuss how the methodology can be further developed and provide a perspective on how the technique could be applied to uncover entirely novel aspects of mechanobiology in the future. Expected final online publication date for the Annual Review of Biophysics, Volume 50 is May 2021. Please see http://www.annualreviews.org/page/journal/pubdates for revised estimates.

Protein Folding Under Mechanical Forces: A Physiological View

Physiology ◽  
2013 ◽  
Vol 28 (1) ◽  
pp. 9-17 ◽  
Author(s):  
Yalda Javadi ◽  
Julio M. Fernandez ◽  
Raul Perez-Jimenez
Keyword(s):  
Protein Folding ◽  
Physiological Significance ◽  
Mechanical Forces

Mechanical forces regulate the function of numerous proteins relevant to physiology. The functions and folding of proteins have been under scrutiny for decades, but it was not until recently that mechanical forces have been considered. Here, we review different techniques for studying protein folding, highlighting their physiological significance.

Photoreactivity Control Mediated by Molecular Force Probes in Stilbene

2019 ◽  
Vol 10 (5) ◽  
pp. 1063-1067 ◽  
Author(s):  
Cristina García-Iriepa ◽  
Diego Sampedro ◽  
Francisco Mendicuti ◽  
Jérémie Léonard ◽  
Luis Manuel Frutos
Keyword(s):  
Molecular Force ◽  
Force Probes

Chemomechanics with molecular force probes

2010 ◽  
Vol 82 (4) ◽  
pp. 931-951 ◽  
Author(s):  
Zhen Huang ◽  
Roman Boulatov
Keyword(s):  
Materials Science ◽  
Reaction Rates ◽  
Restoring Force ◽  
Strained Molecules ◽  
Multiple Length Scales ◽  
Molecular Force ◽  
Directional Motion ◽  
Restoring Forces ◽  
Highly Strained ◽  
Force Probes

Chemomechanics is an emerging area at the interface of chemistry, materials science, physics, and biology that aims at quantitative understanding of reaction dynamics in multiscale phenomena. These are characterized by correlated directional motion at multiple length scales—from molecular to macroscopic. Examples include reactions in stressed materials, in shear flows, and at propagating interfaces, the operation of motor proteins, ion pumps, and actuating polymers, and mechanosensing. To explain the up to 1015-fold variations in reaction rates in multiscale phenomena—which are incompatible within the standard models of chemical kinetics—chemomechanics relies on the concept of molecular restoring force. Molecular force probes are inert molecules that allow incremental variations in restoring forces of diverse reactive moieties over hundreds of piconewtons (pN). Extending beyond the classical studies of reactions of strained molecules, molecular force probes enable experimental explorations of how reaction rates and restoring forces are related. In this review, we will describe the utility of one such probe—stiff stilbene. Various reactive moieties were incorporated in inert linkers that constrained stiff stilbene to highly strained macrocycles. Such series provided the first direct experimental validation of the most popular chemomechanical model, demonstrated its predictive capabilities, and illustrated the diversity of relationships between reaction rates and forces.

ChemInform Abstract: Chemomechanics with Molecular Force Probes

ChemInform ◽  
2010 ◽  
Vol 41 (37) ◽  
pp. no-no
Author(s):  
Zhen Huang ◽  
Roman Boulatov
Keyword(s):  
Molecular Force ◽  
Force Probes

scholarly journals Lipid bilayer regulation of membrane protein function: gramicidin channels as molecular force probes

2009 ◽  
Vol 7 (44) ◽  
pp. 373-395 ◽  
Author(s):  
Jens A. Lundbæk ◽  
Shemille A. Collingwood ◽  
Helgi I. Ingólfsson ◽  
Ruchi Kapoor ◽  
Olaf S. Andersen
Keyword(s):  
Membrane Protein ◽  
Physical Properties ◽  
Lipid Bilayer ◽  
Protein Function ◽  
Elastic Moduli ◽  
Model Systems ◽  
Energetic Cost ◽  
Molecular Force ◽  
Membrane Protein Function ◽  
Force Probes

Membrane protein function is regulated by the host lipid bilayer composition. This regulation may depend on specific chemical interactions between proteins and individual molecules in the bilayer, as well as on non-specific interactions between proteins and the bilayer behaving as a physical entity with collective physical properties (e.g. thickness, intrinsic monolayer curvature or elastic moduli). Studies in physico-chemical model systems have demonstrated that changes in bilayer physical properties can regulate membrane protein function by altering the energetic cost of the bilayer deformation associated with a protein conformational change. This type of regulation is well characterized, and its mechanistic elucidation is an interdisciplinary field bordering on physics, chemistry and biology. Changes in lipid composition that alter bilayer physical properties (including cholesterol, polyunsaturated fatty acids, other lipid metabolites and amphiphiles) regulate a wide range of membrane proteins in a seemingly non-specific manner. The commonality of the changes in protein function suggests an underlying physical mechanism, and recent studies show that at least some of the changes are caused by altered bilayer physical properties. This advance is because of the introduction of new tools for studying lipid bilayer regulation of protein function. The present review provides an introduction to the regulation of membrane protein function by the bilayer physical properties. We further describe the use of gramicidin channels as molecular force probes for studying this mechanism, with a unique ability to discriminate between consequences of changes in monolayer curvature and bilayer elastic moduli.

scholarly journals A Modular Approach to Mechanically Gated Photoswitching with Color-Tunable Molecular Force Probes

2021 ◽  
Author(s):  
Ross W. Barber ◽  
Maxwell J. Robb
Keyword(s):  
Mechanical Stress ◽  
Visual Cues ◽  
Mechanochemical Activation ◽  
Modular Approach ◽  
Molecular Force ◽  
Color Tunable ◽  
Force Probes

Molecular force probes conveniently report on mechanical stress and/or strain in polymers through straightforward visual cues. Unlike conventional mechanochromic mechanophores, the mechanically gated photoswitching strategy decouples mechanochemical activation from the...

scholarly journals Force-Rate Characterization of Two Spiropyran-Based Molecular Force Probes

2015 ◽  
Vol 137 (19) ◽  
pp. 6148-6151 ◽  
Author(s):  
Gregory R. Gossweiler ◽  
Tatiana B. Kouznetsova ◽  
Stephen L. Craig
Keyword(s):  
Molecular Force ◽  
Force Probes
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