Chapter 3 Flashcards
What do amino acids contain?
Carboxy,l Amino, and a hydrogen group
What is the way to differentiate the 20 different amino acids?
the difference is in their side chains
Of the amino acid groups which portion of the structure takes a negative charge?
carboxyl group
What happens when an amino acid is exposed to an aqueous environment?
it gains a proton and takes a positive charge.
What is the largest group of amino acids? (reference to the 20 different kinds)
non polar side chain group
what makes an amino acid polar?
the covalent bonds on the peripheral side allow them to make hydrogen bonds.
Are amino acids bases or acids and strong or weak?
weak acids and bases
basic- if the side chain picks up a proton
acidic- if it contains a carboxyl side chain
What is important of the amino acids side chains?
The properties of their side chain dictate how reactive and soluble they are
How is it easy to get amino acids in the prebiotic earth?
carbon + heat + pressure
What describes the fact that 19/20 amino acids can be found in two ways?
optical isomers, basically asymetry
What is the only amino acid that has one form
Glycine
What way do organisms absorb amino acids (which form)
left handed
What are peptide bonds?
covalent bonds that link amino acids together
What does the vastly differing shapes of proteins have to do with?
The greater the diversity of shape and structure the vastly differing things it can do in terms of function
What are the terminuses of amino acids?
N and C.
Which end do you begin numbering the amino acids?
the N terminus
Describe the primary sequence of protein folding?
the linear structure of amino acids is altered for further folding and is stabilized via peptide bonds
Describe the secondary sequence of protein folding?
the secondary structures are stabilized, while an oxygen and a hydrogen on both ends form hydrogen bond, thus folding the shape.
Describe the tertiary sequence of protein folding?
there is a stabilized shape, resulting from hydrogen bonds, ionic, disulfide bond, van der waals interactions, and other stabilizing forces that form a very diverse and independent structure. The R groups is what is bonded in tis instance.
Describe the quaternary sequence of protein folding?
when two different polypeptides come together to make the final protein
What is protein denaturation?
when the protein unfolds via chemicals in the environment
Intrinsic factors:
inability for polar molecules to form hydrogen bonds
extrinsic factors:
chaperons and chaperonins
What are chapernoes and chaperonins?
chaperons: grab onto unfolded proteins
chaperonins: create a small barrel structure to enclose and randomize/complexify the protein .
