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Related Concept Videos

Mechanical Protein Functions01:58

Mechanical Protein Functions

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Proteins perform many mechanical functions in a cell. These proteins can be classified into two general categories- proteins that generate mechanical forces and proteins that are subjected to mechanical forces. Proteins providing mechanical support to the structure of the cell, such as keratin, are subjected to mechanical force, whereas proteins involved in cell movement and transport of molecules across cell membranes, such as an ion pump, are examples of generating mechanical force. 
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Protein Dynamics in Living Cells01:19

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Different fluorescence-based techniques are used to study the protein dynamics in living cells. These techniques include FRAP, FRET, and PET.
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...
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The Movement of Organelles and Vesicles01:43

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In eukaryotic cells,  cytoskeletal filaments such as actin, microtubules, and intermediate filaments form a mesh-like cytoskeletal network. These filaments serve as tracks for transporting cellular cargo. Specialized motor proteins use the chemical energy stored in adenosine triphosphate (ATP) for this transport. During interphase, microtubules are polarized, with the plus-end towards the cell periphery and the minus-end towards the cell center. Two microtubule-associated motor proteins,...
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Gene Evolution - Fast or Slow?02:05

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The genomes of eukaryotes are punctuated by long stretches of sequence which do not code for proteins or RNAs. Although some of these regions do contain crucial regulatory sequences, the vast majority of this DNA serves no known function. Typically, these regions of the genome are the ones in which the fastest change, in evolutionary terms, is observed, because there is typically little to no selection pressure acting on these regions to preserve their sequences.
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Protein Diffusion in the Membrane01:24

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Proteins show rotational as well as lateral diffusion across the membrane. The lateral diffusion of proteins was confirmed through the cell fusion experiment where mouse and human cells were fused, resulting in hybrid cells. When the human and mouse cells fused, the specific membrane proteins on human and mouse cells were marked with the red and green-fluorescent markers, respectively. Initially, the red and green fluorescence was located on the respective hemisphere of the cell. As time...
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Actin Filament Depolymerization01:19

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Actin filaments (F-actin) are composed of actin subunits. The dissociation of actin monomers can occur from either end of F-actin. The rate of dissociation is faster from the minus-end or the pointed end, where the actin subunits exist with a bound ADP, together known as ADP-actin. The depolymerization of F-actin is aided by proteins, including the actin-depolymerizing factor (ADF) and cofilin family of proteins, gelsolin, and glia maturation factor (GMF).
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Dissecting Mechanoenzymatic Properties of Processive Myosins with Ultrafast Force-Clamp Spectroscopy
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Perspective: How Fast Dynamics Affect Slow Function in Protein Machines.

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This summary is machine-generated.

Protein dynamics are crucial for function, involving both equilibrium fluctuations and energy-driven, out-of-equilibrium processes. This two-time-scale model explains how fast motions and slower functional transitions in protein machines are coupled.

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Using In Vitro Fluorescence Resonance Energy Transfer to Study the Dynamics Of Protein Complexes at a Millisecond Time Scale
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Area of Science:

  • Biophysics
  • Biochemistry
  • Protein Dynamics

Background:

  • Protein internal motions occur across diverse timescales and spatial scales.
  • The coupling of protein dynamics to biochemical function is a long-standing question in biophysics.
  • Proposed mechanisms include equilibrium concepts like dynamic allostery and out-of-equilibrium operations.

Purpose of the Study:

  • To explore mechanisms coupling protein dynamics to biochemical function.
  • To discuss experimental studies demonstrating out-of-equilibrium processes in protein function.
  • To propose a novel two-time-scale paradigm for protein machine activity.

Main Methods:

  • Review and discussion of recent experimental studies.
  • Analysis of Brownian ratchet mechanisms involving energy input.
  • Examination of enzyme dynamics, such as microsecond domain closure, affecting slower chemical cycles.

Main Results:

  • Demonstration of dynamic allostery through modulation of protein entropy affecting binding.
  • Evidence for out-of-equilibrium mechanisms, like Brownian ratchets, driving directional protein motion.
  • Observation of microsecond domain dynamics influencing enzyme catalytic cycles.

Conclusions:

  • A novel two-time-scale paradigm for protein machine activity is proposed.
  • This paradigm involves fast equilibrium fluctuations (microsecond-millisecond) and slower, energy-driven functional transitions.
  • Interplay between fast and slow motions is essential for protein machine function.