The conversion of cysteine to cystine is what kind of reaction? an oxidation a r

Question

The conversion of cysteine to cystine is what kind of reaction? an oxidation a reduction an addition a condensation a hydrolysis Which of the following is NOT true of peptide bonds? They tend to be planar. They are generally in the trans and rarely in the cis configuration. They tend to have the amide nitrogen protonated to give a positive charge. They contain an unusually long carbon-carbon bond. What do alpha-helices and beta-sheets have in common? Both are stabilized by hydrogen bonding involving carbonyl oxygens and amide nitrogens. The same amino acids stabilize both forms of secondary structure. The length of a 10-amino acid alpha-helix and beta-sheet strand will be the same. Both are stabilized by glycine and proline residues. Water-soluble proteins such as myoglobin tend to fold such that hydrophobic amino acid R-groups are on the interior of the protein and hydrophilic groups are on the outside. hydrophilic amino acid R-groups are on the interior of t

Explanation / Answer

1) an oxidation

reason -SH and -SH bonds of two cysteine combine to form disulfide bond -S-S- giving away hydrogen atoms H+ and two electrons)

2) peptides bonds are generally in trans and rarely in cis configuration

reason-more favorable trans ,less steric crowding

3)a) Both are stabilised by Hydrogen bonding involving carbonyl oxygen and amide nitrogen

in beta pleated ,hydrogen bonding occurs between CO and NH of two different peptide strand while in the former it occurs in one strand of peptide

4)hydrophobic amino acid R-groups are on the interior of the protein and hydrophillic groups are on the outside

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