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47 Cards in this Set

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What are the nine hydrophobic amino acids?.... why are these important
glycine, alanine, valine, leucine, isoleucine, proline, phenylalanine, tyrosine, tryptophan.... These amino acids will most likey be used in the N-terminus of the secreted protein, such as insulin, or membrane or organelle protein
What are the 6 nonpolar, amino acids with aliphatic side chains?
glycine, alanine, valine, leucine, isoleucine, proline
What re the 3 amino acids with aromatic side chains ?
phenylalanine, tyrosine, tryptophan
What is the smallest amino acid?
Which amino acids will disrupte the alpha helixes of membranes?
glycine, because it is so small... proline , because it’s R group is attached to it’s amino group.
What are the amino acids with branched chains?... Why are these important?
Leucine... Isoleucine... Valine... These amino acids require BRANCHED CHAIN DEHYDROGENASE which is DEFICIENT IN MAPLE SYRUP URINE DISEASE
What is the difference between penylalanine and tyrosine?
OH group is on the aromatic ring of tyrosine, while it is absent on phenylalanine
What is the only amino acid with a phenol group
What is tyrosine a precursure of?
thyroid hormone, catacholamines, melanin
What is needed for the conversion of tyrosine to catachole?
addition of another OH group to the already present phenol on the tyrosine?
What is tryptophan used for?
major procurer of serotonin, and is used for NAD and NADP synthesis
What are the hydrophilic amino acids?
lysine, arginine, histidine, aspartate, glutamate, serine, threonine, cysteine, methionine, asparagine, glutamine
Which amino acids have positively charged R groups?
lysine, arginine, histidine
Which amino acids have negatively charged R groups?
aspartate glutamate
Which amino acids have polar, uncharged R groups?
serine, threonine, cysteine, methionine, asparagine, glutamine
What gives the positively charged amino acids their charge?
an extra amino group
Which amino acids would be abundant in histones?
lysine and arginine because it is a positively charged protein
Where is the amino group on lysine?
it is on the very end of the R group…this position is known as the epsilon position
Why is the epsilon position on amino acid important?
it is on the epsilon amin o group of lysine that glycosylation of hemoglobin occurs
What gives the negatively charged R groups their negative charge?
Their side chains contain an extra carboxylic acid group
What is the significance of both negatively charged amino acids?
Aspartate and glutamate are both excitatory neurotransmitters in the CNS………………….glutamate is also a precursor of GABA.
Which amino acid is notorious for being a great physiological buffer?
Which amino acids contain S in their side chains?
cysteine and methionine
Which amino acids has an SH at the end of its side chain and why is this important?
cysteine….it is pmportant because it is between these SH group that disulfide bonds between proteins are made…..this SH group on cysteine in the protein glutathione which mops up free redicals
Which amino acids have an extra OH group in the side chain?
serine, threonine
What is the importance of the OH groups on the proteins?
These are sites where posttranslation al modification can perform glycosylation and phosphorylation of protein.
What medication is given to people experiencing free radical damage, such as Tylenol or acetomeniphen overdose?
What is the importance of methionine?
it is a key methyl group donator and thus is a main component of the SAM enzyme.
What is the name of the proteins that wraps up free radicals in cells and what is this due to?
glutathione mops up free radicals and it is due to the SH bonds on cysteins amino acids in the protein
What are some key reactions of the SAM protein?
methylation of norepinephrine to epinephrine……………..or adding a methyl to the guanine to form the methyl guanine cap.
What is the importance of asparagine and glutamine?
These proteins have H2N on the end of their R group and thus allow N glycosylation of the end of their side chains
What is the importance of glutamine?
it can detoxify ammonia due to the activity of glutamine synthetase
What is the pK value for the amino group on amino acids?
What is the pK value for the acid group on amino acids?
What are the positively chargesd amino acids and what is the pK of their extra amino group?
arginine = 13... Lysine = 10... Histadine = 6.5
What are the negatively charged amino acids and what is the pK of their extra acid groups?
Aspartate = 4... glutamate = 4
What is an isoelectric point of a molecule?
this is the oint at which the pH and PK is balanced and there is no overall charge on the molecule , and thus it will not migrate the positive or negative electrode
What is a characteristic of asprin and how is this used?
asprin is a weak acid and thus is order to make it more water soluble, the urine is alkalized and that asprin gains a charge and dissolves in water. When a weak acid is in acid, it is uncharged, and thus not soluble in water, but if the weak acid is in basic solution it will lose it H+, gain a neg. charge and thus become soluble.
What is a quick way to find the approximate pK?
average the two closest pKs.
Why is histidine such a good buffer?
it has the third pK at a value of 6.5
What are the important intracellular buffers?
Proteins (due to histidine R groups).... Phosphate.... Organic phosphates
What is an important extracellular buffer?
bicarbonate, the most important buffer
What are the ten essential amino acids?
PVT TIM HALL ………Phenylalanine…………Valine………….. Tryptophan…... Threonine…………Isoleucine ……Methionine ……….Histidine.... Arginine………..Leucine…….Lysine
What of the essential amino acids are only required during period of growth?
What is a negative nitrogen balance?
When the losses exceed the amount of nitrogen input.
What is the main parameter of the energy of a reaction?
delta G….negative delta G means that there is an energy loss and thus it is spontaneous….but tells nothing at all about the rate
What are the parameters of the rate of a reaction?
Km and Vmax