Prion diseases are caused by—     protein misfolding.     protein “melting” under heat shock.     protein degradation.     protein denaturation.     protein disintegration

What is the denaturant in Anfinsen’s classic experiment to demonstrate that reduced and denatured RNase A could refold into the native form?     Urea.     GroEL.     2-mercaptoethanol.     Heat shock protein.     Protein disulfide isomerase.

Each one gives some basic information and summarizes its main role in translation. mRNA:       Ribosome:

Alpha-helices and beta-pleated sheets are formed during this stage of protein folding.     Secondary     Primary     Tertriary     Quanternary

What general structural feature is shared by proteins that specifically form homodimers (but not homotrimers, homoteramers etc)? Only one answer is correct.     the surface consists of hydrophilic alpha-helix.   the surface is highly modified by post-translational modification.   the surface is permanently bound by chaperones.   the surface is unstructured.   the surface, or part of it, is self-complementary.

The human anti-bacterial protein lysozyme, consisting of a single polypeptide with 129 amino acids, contains how many peptide bonds? 131 peptide bonds 130 peptide bonds 129 peptide bonds 128 peptide bonds 127 peptide bonds