ch 1 amino acids, peptides, proteins

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Biochemistry Fichas sobre ch 1 amino acids, peptides, proteins, creado por ajf el 18/08/2015.
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Pregunta Respuesta
the AA carbon with the R-group or side-chain is called what? alpha carbon
which AA is achiral? glycine
all AA are what configuration (R/S)? L/D configuration? all AA are (S)-configured, with the exception of cysteine (R); all AA are levorotatory (L)
name the seven (7) non-polar AA glycine, alanine, valine, leucine, isoleucine, methionine, proline
which AA contain sulfur? cysteine, methionine
name the three (3) AA with aromatic side chains tryptophan, phenylalanine, tyrosine
name the five (5) AA with polar side chains (but not acidic/basic) serine, threonine, asparagine, glutamine, cysteine
name the negatively charged (acidic) AA aspartic acid (aspartate), glutamic acid (glutamine)
list the positively charged (basic) AA lysine, arginine, histadine
are hydrophobic AA found near the exterior or interior or proteins? hydrophilic AA? hydrophobic found in the interior; hydrophilic found in the exterior; all others found in between
what is an amphoteric species? molecule or ion that can react as an acid as well as a base
what signifies: [HA] = [A-] pKa
pKa of carboxyl group? ~2-5
pKa of amino group? ~9-10
in an acidic environment (low pH), are AA positively or negatively charged? in a basic environment (high pH), are AA positively or negatively charged? acidic pH = positively charged AA basic pH = negatively charged AA
what's a zwitterion? is a neutral molecule with a positive and a negative electrical charge, also known as dipolar ion
a buffer is when _____ is close to the pKa value pH
what is the isoelectric point (pI)? is the pH at which a particular molecule carries no net electrical charge
(equation for) pI of neutral AA? (pH = ~6) = pKa of NH3(+) plus pKa of COOH divided by two
(equation for) pI of acidic AA? = pKa of R-group plus pKa of COOH divided by two
(equation for) pI of basic AA? = pKa of R-group plus pKa of NH3(+) divided by two
what are peptides called with up to 20 amino acids subunits? oligopeptides
what are peptides called with more than 20 amino acids subunits? polypeptides
what's the free amino acid end called? N-terminus
what's the free carboxyl end called? C-terminus
define protein's primary structure linear arrangement of amino acids (N-terminus to C-terminus)
define protein's secondary structure alpha-helices: peptide chain coiled in a clock-wise fashion; side chain points away from the core beta-helices: pleated sheets (rippled) that can be parallel or antiparallel
define protein's tertiary structure 3-D shape, determined by hydrophilic/hydrophobic interactions of R-groups disulfide bonds (salt-bridges) form w/two cysteine molecules become oxidized to form cystine
molten globules intermediate states in protein folding
negative S or entropy is? increasing order
with respect to hydrophilic AA, entropy is increased or decreased? delta S is positive; order is decreased
define protein's quaternary structure (not all proteins have this structure) aggregate of smaller globular peptides from induced allosteric effects and cooperativity (example: hemoglobin, antibodies)
what kind of reaction is breaking a peptide bond? hydrolysis
which AA interrupts secondary structure because of its rigid cyclic structure? proline
what's a conjugated protein? protein with covalently attached prosthetic group
what's a prosthetic group? give some examples cofactor -- metal ion, vitamin, lipid, carbohydrate, or nucleic acid
denaturation pH, salinity, high temp lead to loss of 3D shape of protein (unravels); increases KE
in neutral solution, most amino acids exist as what? zwitterions (except the acidic and basic amino acids)
at neutral pH 7, the charge on glutamic acid is what? net charge of -1 (remains protonated at pH 7)
nonpolar R groups in aqueous solution are hydrophilic/hydrophobic and found on the surface/interior of protein? hydrophobic/interior
what type of reaction forms a peptide bond? condensation -- specifically dehydration, involving the loss of water
which structures (primary, secondary,tertiary, quaternary) are preserved during protein denaturation? primary only (AA chain not broken)
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