Lecture 5 protein structure and function

What primary function do carbohydrates play in biological systems, as highlighted in the provided context?

Which molecule is described as offering a dynamism unseen in other biological macromolecules?

What is the central role of mRNA in gene expression, as inferred from the text provided?

According to the provided text, what aspect of macromolecules in biology is tightly correlated to their function?

In the 'pre-life RNA world,' what best describes the function that RNA fulfilled?

What is the primary cause of diseases such as Alzheimer's, Parkinson's, and Huntington's?

What is the name of the bond formed when two amino acids are joined?

Where is the polypeptide sequence ultimately determined?

What is the term for a chain of amino acids containing just a few residues?

How are the side chains arranged in a primary structure?

Which method for determining protein structure does not require protein crystallization?

What is a primary advantage of using artificial intelligence in bioinformatics for protein structure prediction?

What distinguishes antiparallel β sheets from parallel β sheets?

Which resource would be most helpful to use when searching for a specific peer-reviewed research article about protein structure?

Why is understanding a protein’s structure considered important?

Which type of protein structure is most directly associated with the formation of amyloid structures?

Where would you look to find examples of general protein functions?

What is a key factor determining a protein's tertiary structure?

What type of bond, crucial for the stability of some proteins like antibodies, is formed between cysteine residues?

If a protein containing disulfide bridges is boiled, how would this most likely affect its structure?

During protein synthesis, where are amino acids added to the growing polypeptide chain?

What type of bond is primarily responsible for the formation of secondary structures in proteins?

Which of the following best describes the typical structure of an alpha helix?

Which secondary structure is frequently found in membrane-bound proteins when crossing the lipid bilayer?

What term describes the flexible regions of a polypeptide that connect structured domains?

Why is secondary structure in proteins generally consistent?

What is the key difference between asparagine/glutamine and aspartate/glutamate?

What kind of structure can be formed by intertwined alpha helices?

Why does phosphorylation of serine, threonine, or tyrosine affect a protein's function?

What are the two ends of the growing polypeptide chain called?

Which characteristic makes serine, threonine, and tyrosine hydrophilic?

What is a key structural feature of cysteine that is important for protein function?

What kind of bonds can acidic amino acid side chains form within a cell?

How do acidic amino acid side chains enhance the water solubility of a polypeptide?

How do basic amino acid side chains contribute to a polypeptide's structure and function?

How do proteins typically achieve their lowest energy conformation during synthesis?