Chaperones and chaperone-substrate complexes: Dynamic playgrounds for NMR spectroscopists
Björn M Burmann1, Sebastian Hiller1
1Biozentrum, University of Basel, Klingelbergstrasse 70, 4056 Basel, Switzerland.
Progress in Nuclear Magnetic Resonance Spectroscopy
|April 29, 2015
Summary
Molecular chaperones prevent protein misfolding and aggregation. Nuclear Magnetic Resonance (NMR) spectroscopy reveals the dynamic structures of chaperone-substrate complexes, offering atomic-level insights into their protective functions.
Area of Science:
- Biochemistry and Molecular Biology
- Structural Biology
Background:
- Proteins require specific 3D structures for function.
- Molecular chaperones are essential cellular machinery guiding protein folding and preventing aggregation.
- Cellular chaperone networks manage protein transport, folding, unfolding, aggregate resolution, and proteolysis.
Purpose of the Study:
- To review the application of NMR spectroscopy in understanding chaperone function.
- To elucidate the structural basis of chaperone-substrate interactions.
- To highlight recent atomic-resolution structural insights into chaperone-substrate complexes.
Main Methods:
- Nuclear Magnetic Resonance (NMR) spectroscopy is employed to study dynamic chaperone-substrate complexes.
- Various NMR techniques are assessed for their utility in characterizing chaperones and their complexes.
- Case studies of recent NMR investigations are presented.
Main Results:
- NMR spectroscopy is a powerful tool for characterizing highly dynamic chaperone-substrate interactions.
- Recent studies using NMR have provided atomic-resolution structures of these complexes.
- This structural information is crucial for understanding how chaperones protect substrates.
Conclusions:
- NMR spectroscopy overcomes crystallization challenges, enabling the study of dynamic chaperone-substrate complexes.
- Structural insights from NMR advance our understanding of chaperone-mediated protein quality control.
- This review emphasizes the critical role of NMR in deciphering chaperone mechanisms.
Related Concept Videos
03:00Molecular Chaperones and Protein Folding
21.0K
The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
The...
21.0K
03:00Molecular Chaperones and Protein Folding
15.7K
15.7K
00:52¹H NMR of Conformationally Flexible Molecules: Temporal Resolution
1.4K
At room temperature, the chair conformer of cyclohexane undergoes rapid ring flipping between two equivalent chair conformers at a rate of approximately 105 times per second. These two chair conformers are in equilibrium. The rapid ring flipping results in the interconversion of the axial proton to an equatorial proton and an equatorial to the axial proton. Such interconversions are too rapid and cannot be detected on the NMR timescale. Hence, the NMR spectrometer cannot distinguish between the...
1.4K
01:192D NMR: Heteronuclear Single-Quantum Correlation Spectroscopy (HSQC)
1.7K
Heteronuclear single-quantum correlation spectroscopy (HSQC) is a 2D NMR technique that reveals one-bond correlations between hydrogen and a heteronucleus. The HSQC experiment is similar to the heteronuclear correlation experiment (HETCOR) but is more sensitive. In the HSQC spectrum, the proton chemical shift is plotted on the horizontal F2 axis, while the 13C chemical shift is plotted on the vertical F1 axis. The corresponding proton and 13C spectra are also shown. The HSQC contour plot does...
1.7K
01:182D NMR: Overview of Heteronuclear Correlation Techniques
930
Heteronuclear correlation spectroscopy is an analytical technique that investigates the coupling between different types of nuclei, often a proton and an X-nucleus, such as carbon-13 or nitrogen-15. This method is commonly used in nuclear magnetic resonance (NMR) spectroscopy to gain insights into complex chemical compounds' structural and compositional aspects. A typical heteronuclear correlation spectrum displays X-nucleus chemical shifts on one axis and a proton spectrum on the other...
930
01:02¹H NMR: Interpreting Distorted and Overlapping Signals
1.8K
Spin systems where the difference in chemical shifts of the coupled nuclei is greater than ten times J are called first-order spin systems. These nuclei are weakly coupled, and their chemical shifts and coupling constant can generally be estimated from the well-separated signals in the spectrum.
As Δν decreases and the signals move closer, the doublets appear increasingly distorted. The intensities of the inner lines increase at the cost of those of the outer lines as the signals are...
As Δν decreases and the signals move closer, the doublets appear increasingly distorted. The intensities of the inner lines increase at the cost of those of the outer lines as the signals are...
1.8K