Related Experiment Video
Updated: Jul 30, 2026
06:59
Nanomanipulation of Single RNA Molecules by Optical Tweezers
Published on: August 20, 2014
[Thermodynamic study of guanylspecific ribonuclease C2]
Biofizika
|May 1, 1980
Summary
Guanylspecific RNAse C2 exists as monomers and dimers in solution. Phosphate ions stabilize the enzyme and promote a monomeric form, impacting its thermodynamic properties.
Area of Science:
- Biochemistry
- Enzymology
- Protein Thermodynamics
Context:
- Guanylspecific RNAse C2 is an enzyme with potential biological significance.
- Understanding protein quaternary structure and stability is crucial in biochemistry.
- Microcalorimetry is a key technique for studying biomolecular interactions and stability.
Purpose:
- To thermodynamically characterize Guanylspecific RNAse C2.
- To investigate the influence of pH on RNAse C2 structure.
- To determine the effect of phosphate ions on RNAse C2 stability and form.
Summary:
- Thermodynamic studies using microcalorimetry reveal that Guanylspecific RNAse C2 exists in a pH range of 5.0-8.0 as a mixture of approximately 30% monomer and 70% dimer.
- Both monomeric and dimeric forms of RNAse C2 exhibit cooperative melting, indicating stable structural units.
- Phosphate ions were found to stabilize the RNAse C2 system by 3-4 degrees Celsius and induce a shift towards the monomeric form.
Impact:
- Provides fundamental thermodynamic data for Guanylspecific RNAse C2.
- Elucidates the pH-dependent quaternary structure of the enzyme.
- Demonstrates the stabilizing effect of phosphate ions and their role in modulating enzyme oligomerization.
Related Concept Videos
01:44Termination of Translation
The large ribosomal subunit has several important structures essential to translation. These include the peptidyl transferase center (PTC) - which is the site where the peptide bond is formed - and a large, internal, water-filled tube through which the nascent polypeptide moves. This latter structure is called the Peptide Exit Tunnel, and it begins at the PTC and spans the body of the large ribosomal subunit. During translation, as the nascent polypeptide chain is synthesized, it passes through...
02:28Leaky Scanning
During most eukaryotic translation processes, the small 40S ribosome subunit scans an mRNA from its 5' end until it encounters the first start AUG codon. The large 60S ribosomal subunit then joins the smaller one to initiate protein synthesis. The location of the translation initiation is largely determined by the nucleotides near the start codon as there may be multiple translation initiation sites present on the mRNA. Marilyn Kozak discovered that the sequence RCCAUGG (where R stands for...
02:47Ribozymes
The term ribozyme is used for RNA that can act as an enzyme. Ribozymes are mainly found in selected viruses, bacteria, plant organelles, and lower eukaryotes. Ribozymes were first discovered in 1982 when Tom Cech’s laboratory observed Group I introns acting as enzymes. This was shortly followed by the discovery of another ribozyme, Ribonulcease P, by Sid Altman’s laboratory. Both Cech and Altman received the Nobel Prize in chemistry in 1989 for their work on ribozymes.
Ribozymes can be...
Ribozymes can be...
02:24Ribosome Profiling
Ribosome profiling or ribo-sequencing is a deep sequencing technique that produces a snapshot of active translation in a cell. It selectively sequences the mRNAs protected by ribosomes to get an insight into a cell’s translation landscape at any given point in time.
Applications of ribosome profiling
Ribosome profiling has many applications, including in vivo monitoring of translation inside a particular organ or tissue type and quantifying new protein synthesis levels.
The technique helps...
Applications of ribosome profiling
Ribosome profiling has many applications, including in vivo monitoring of translation inside a particular organ or tissue type and quantifying new protein synthesis levels.
The technique helps...
02:47Ribozymes
The term ribozyme is used for RNA that can act as an enzyme. Ribozymes are mainly found in selected viruses, bacteria, plant organelles, and lower eukaryotes. Ribozymes were first discovered in 1982 when Tom Cech’s laboratory observed Group I introns acting as enzymes. This was shortly followed by the discovery of another ribozyme, Ribonulcease P, by Sid Altman’s laboratory. Both Cech and Altman received the Nobel Prize in chemistry in 1989 for their work on ribozymes.
Ribozymes can be...
Ribozymes can be...
01:29Translational Regulation
Translational regulation in prokaryotes ensures efficient protein synthesis by controlling ribosome access to mRNA. This regulation is mediated by secondary RNA structures, including translational riboswitches, RNA thermometers, and small RNAs (sRNAs), which respond to intracellular and environmental signals to modulate gene expression.Translational RiboswitchesRiboswitches in the leader region of mRNAs can regulate translation by altering the accessibility of the Shine-Dalgarno (SD) sequence,...