Secondary/ tertiary structure of proteins

In summary: So overall, the tertiary structure is a result of a combination of free energy, hydrophobicity, and interaction between the side chains. In summary, the tertiary structure of a protein is a result of the interaction between the side chains.
  • #1
Cheman
235
1
Why does the secondary/ tertiary structure of a protein exist? Is it due to the fact that all the bonds in polypeptide are not straight as we tend to draw them? ie - bond angle, such as the 109.5 degrees for C-C, exist and also bonds are free to rotate unless hydrogen bonds are present. (as they are in polypeptides.)

Thanks in advance. :rofl:
 
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  • #2
the so-called "weak forces" are responsible for giving a complex molecule it's conformation. note that there isn't necessarily one fixed conformation, but a probability based upon the total energy of the molecule. the lowest energy state is generally considered to be the true conformation, but this is not always true in living systems.

obviously the bond angle of a peptide bond (and rotation around it) will influence this, but the weak force interactions between the amino acid side chains is primarily responsible for giving the protein its conformation.

actually computing these conformations based upon the amino acid sequence is an incredibly difficult challenge, as you can probably imagine.
 
  • #3
Sulfur bridges play an important role in protein folding, also weak forces such as ionic bonds, van der Waals forces, hydrogen bonds, burying of non-polar side chains etc.
 
  • #4
In order to understand why secondary structures occur such as two of the more ubiquitous secondary structures (alpha helix and the beta sheets) one must understand the hydrophobic effect. I can expand on this if someone requests but basically the hydrophobic sidechains tend to be buried in the core of the protein and the hydrophilic amino acid sidechains tend to be exposed on the surface-water interface. One then may say, "Well so what if the side chain is nonpolar/hydrophobic all amino acids are composed of a polar carboxyl and amino component." So nature has a way of satisfying all these polar groups with hydrogen bonds through secondary structures such as alpha helices and beta sheets.
 
  • #5
Cheman said:
Why does the secondary/ tertiary structure of a protein exist? QUOTE]

The tertiary structures of a protein or the three dimensional shape a protein takes in solution is basically a thermodynamically driven process. There is one shape that the protein can assume where its Gibbs free energy will be the most negative. So just think of all the amino acid sidechains rotating and bending into a final conformation where the free energy is at a minimum. This process is directly dependent on the environment or the solution the protein! For example at very high temperatures the tertiary structure is different then it is in physiological conditions, it is generally "denatured" or not in its native state. This just means that it is not in the same fold it is in physiological conditions. Also remember that a proteins tertiary structure, like most biochemical phenamena, is not static. It is constantly "breathing" or moving due to side chain rotations etc.
 

1. What is the difference between secondary and tertiary structure of proteins?

The secondary structure of proteins refers to the local folding of the polypeptide chain into alpha helices, beta sheets, or other stable structures. On the other hand, tertiary structure refers to the overall 3D arrangement of the entire protein molecule, including the interactions between different secondary structures. In simpler terms, secondary structure is like individual building blocks, while tertiary structure is the final structure of the entire protein.

2. How is the secondary structure of proteins determined?

The secondary structure of proteins can be determined experimentally through techniques such as X-ray crystallography, nuclear magnetic resonance (NMR) spectroscopy, and circular dichroism (CD) spectroscopy. These methods allow scientists to visualize the arrangement of atoms and bonds in the protein, which can then be used to determine the secondary structure.

3. What are the main forces that contribute to the stability of tertiary structure?

The main forces that contribute to the stability of tertiary structure include hydrogen bonding, hydrophobic interactions, electrostatic interactions, and disulfide bonds. These forces help to hold the secondary structures in place and maintain the overall 3D shape of the protein.

4. How does the tertiary structure of a protein affect its function?

The tertiary structure of a protein is crucial for its function, as it determines the specific shape and surface features of the protein. These features allow the protein to interact with other molecules and perform its specific biological function. Any changes in the tertiary structure can alter the function of the protein and potentially lead to disease or dysfunction.

5. Can the tertiary structure of a protein change?

Yes, the tertiary structure of a protein can change under certain conditions. For example, changes in pH, temperature, or exposure to certain chemicals can cause the protein to unfold or denature, disrupting its tertiary structure. However, in some cases, proteins can also refold and regain their tertiary structure under favorable conditions.

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