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Related Concept Videos

Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
Protein Dynamics in Living Cells01:19

Protein Dynamics in Living Cells

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...
Phase Transitions: Melting and Freezing02:39

Phase Transitions: Melting and Freezing

Heating a crystalline solid increases the average energy of its atoms, molecules, or ions, and the solid gets hotter. At some point, the added energy becomes large enough to partially overcome the forces holding the molecules or ions of the solid in their fixed positions, and the solid begins the process of transitioning to the liquid state or melting. At this point, the temperature of the solid stops rising, despite the continual input of heat, and it remains constant until all of the solid is...
Bacterial Protein Maturation01:26

Bacterial Protein Maturation

Bacterial protein maturation is a tightly regulated process that ensures newly synthesized polypeptides achieve correct functional conformations. This maturation involves a series of modifications, folding events, and quality control steps, often assisted by specialized chaperone proteins.N-Terminal ModificationsThe maturation of bacterial polypeptides begins cotranslationally as the polypeptide exits the ribosome. The first amino acid, N-formylmethionine (fMet), is typically modified at the...

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NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins
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Protein dynamical transition at 110 K.

Chae Un Kim1, Mark W Tate, Sol M Gruner

  • 1Cornell High Energy Synchrotron Source, Laboratory of Atomic and Solid State Physics, and Department of Physics, Cornell University, Ithaca, NY 14853, USA. ck243@cornell.edu

Proceedings of the National Academy of Sciences of the United States of America
|December 15, 2011
PubMed
Summary
This summary is machine-generated.

A protein dynamical transition was observed at 110 K, significantly lower than previously known. This transition correlates with water

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Area of Science:

  • Biophysics
  • Physical Chemistry
  • Materials Science

Background:

  • Proteins exhibit a known dynamical transition around 200 K, but its mechanism and link to water remain debated.
  • Understanding protein dynamics is crucial for various biological and chemical processes.

Purpose of the Study:

  • To investigate the protein dynamical transition at temperatures lower than previously reported.
  • To explore the relationship between protein dynamics and the phase transitions of water at cryogenic temperatures.

Main Methods:

  • Experimental observation of protein dynamical transitions.
  • Cryogenic measurements of water phase transitions (high-density amorphous to low-density amorphous states).

Main Results:

  • An unexpected protein dynamical transition was observed at temperatures as low as 110 K.
  • This low-temperature transition precisely correlated with the cryogenic phase transition of water.
  • Observed correlation between protein dynamics and water's amorphous phase transition.

Conclusions:

  • The cryogenic protein dynamical transition may be directly linked to the existence of two distinct liquid forms of water at low temperatures.
  • Findings suggest a significant role for water's structural states in modulating protein dynamics.