Something Else
by Nin Andrews
Sometimes you say I'm something else,
and you mean I'm good, really good,
but honey, don't say that, please?
Reminds me how my dad used to say,
I'm just not myself today.
As if he were some kind of imposter dad.
Then he'd ask things like:
Why don't you go play with James?
Has the dog had his walk yet?
Will you kindly get out of my cotton-pickin' hair?
Sometimes he'd come home from work
carrying his hat and a brown paper bag,
and I'd know he wasn't my dad.
There were at least three daddies then,
sort of like daddy A, B, and C.
Like that TV show. Which will it be,
bachelor number 1, 2, or 3?
My mom often said he wasn't the man
she married. And I thought about that.
How, when they married,
I wasn't me, either. I wasn't anyone.
I didn't like to dwell on that.
It kind of gave me the creeps,
but I liked to ask,
Were you really in love then?
Of course, she'd say.
Did you hold hands?
Yes.
Kiss in public? Sit on his lap?
Yes, yes, I did all that. Once.
She even showed me photos
she kept in her lingerie drawer
beneath her slips and silky things
she never wore anymore: him
in his spats and slick-shined hair,
her in a pink crinoline cocktail dress
with her long bangs clipped back
in pearly barrettes. Not a thought
in her head, except maybe
Don't I look swell? And
Love me. And he did.
Did he say so?
He said it every day.
He was something else back then.
Wednesday, January 27, 2010
I heard this poem today and felt transported into its world.
Tuesday, January 26, 2010
Monday, January 18, 2010
Sunday, January 17, 2010
Tuesday, January 12, 2010
Monday, January 11, 2010
Met756Val
Methionine
Valine
Both of these amino acids are nonpolar and neutral, but valine is more hydrophobic than methionine and that could cause a change in protein function.
Sunday, January 10, 2010
FAMILY/ The Italian Doctors Are Mutating The Gene In a Dish
All proteins are long chains of amino acids. An amino acid, in general, looks like this:
The "R" in a box represents the variable group. Differences in the R group are how we get the twenty-two standard amino acids we use to make the proteins in our body that are responsible for every thing from muscles to the channels in the membranes of neurons that allow us to think and move.
The NH2 shown on the left is an amine group, and the COOH shown on the right is a carboxylic acid group - this is how the amino acid got its name. When you line the carboxylic acid end (C terminus) of one amino acid up with the amine end (N terminus) of another amino acid, an OH comes off of the carboxylic acid, and an H comes off of the amine. The OH and the H come together to form water, and what's left of the carboxylic acid and the amine come together to form the peptide bond, like this:
Our genes/DNA are what give the protein manufacturing infrastructure in our cells the information for what particular amino acids to string together to make the very specific proteins we need for every biological task we carry out. The string of amino acids, held together by peptide bonds, that make up a particular protein is referred to as its primary structure. More complex interactions between the amino acids allow proteins to have secondary, tertiary, and quaternary structure, as well, so one chain of amino acids can fold itself up into an intricate shape.
Many of the important protein structures in our body are made of several individual proteins interacting. (This interaction is the definition of quaternary structure.) This is the case for the hERG protein, a potassium ion channel that allows the heart to end each heartbeat and get ready for the next at an appropriate rate and rhythm. That process in the heartbeat can be called ventricular repolarization, and on an ECG it is referred to as the QT interval:
The KCNH2 gene is the location on the DNA map that tells the protein manufacturing infrastructure in our cells how to make the largest part of the hERG potassium channel. Different mutations in this gene can cause the QT interval to be either too long, lasting more than 430 milliseconds (Long QT sydrome, specifically LQT2) or too short, lasting less than 300 ms (Short QT syndrome, specifically SQT1). Long QT syndrome is more common than Short QT syndrome. Which one does our Chemical's family have?
SQT1 is caused by replacing the amino acid asparagine in position 588 in the chain with the amino acid lysine. The big difference between these amino acids is that asparagine is neutral, not positively or negatively charged, while lysine is positively charged. The images below don't show where the charge is. I haven't figured that out yet.
asparagine
lysine
The differences in charge and shape between these two amino acids change the way the long chain is able to fold. This one change in primary structure ends up changing the secondary, tertiary, and quaternary levels of structure in the entire hERG potassium channel. Just like everything else in life, a change in structure is also a change in function. For SQT syndrome, this change results in a faster passage of potassium through the channel out of the cardiac cell - a gain of function - that makes the ventricles able to contract before they have enough time to fill with blood.
There seem to be multiple mutations between positions 35 and 36 on chromosome 7 that can cause LQT2. These mutations cause a loss of function in the hERG potassium channel, reducing the rate at which potassium can leave the cell. This makes the ventricles unable to contract when they should because they take too long getting back to their baseline potassium levels.
The "R" in a box represents the variable group. Differences in the R group are how we get the twenty-two standard amino acids we use to make the proteins in our body that are responsible for every thing from muscles to the channels in the membranes of neurons that allow us to think and move.
The NH2 shown on the left is an amine group, and the COOH shown on the right is a carboxylic acid group - this is how the amino acid got its name. When you line the carboxylic acid end (C terminus) of one amino acid up with the amine end (N terminus) of another amino acid, an OH comes off of the carboxylic acid, and an H comes off of the amine. The OH and the H come together to form water, and what's left of the carboxylic acid and the amine come together to form the peptide bond, like this:
Our genes/DNA are what give the protein manufacturing infrastructure in our cells the information for what particular amino acids to string together to make the very specific proteins we need for every biological task we carry out. The string of amino acids, held together by peptide bonds, that make up a particular protein is referred to as its primary structure. More complex interactions between the amino acids allow proteins to have secondary, tertiary, and quaternary structure, as well, so one chain of amino acids can fold itself up into an intricate shape.
Many of the important protein structures in our body are made of several individual proteins interacting. (This interaction is the definition of quaternary structure.) This is the case for the hERG protein, a potassium ion channel that allows the heart to end each heartbeat and get ready for the next at an appropriate rate and rhythm. That process in the heartbeat can be called ventricular repolarization, and on an ECG it is referred to as the QT interval:
The KCNH2 gene is the location on the DNA map that tells the protein manufacturing infrastructure in our cells how to make the largest part of the hERG potassium channel. Different mutations in this gene can cause the QT interval to be either too long, lasting more than 430 milliseconds (Long QT sydrome, specifically LQT2) or too short, lasting less than 300 ms (Short QT syndrome, specifically SQT1). Long QT syndrome is more common than Short QT syndrome. Which one does our Chemical's family have?
SQT1 is caused by replacing the amino acid asparagine in position 588 in the chain with the amino acid lysine. The big difference between these amino acids is that asparagine is neutral, not positively or negatively charged, while lysine is positively charged. The images below don't show where the charge is. I haven't figured that out yet.
asparagine
lysine
The differences in charge and shape between these two amino acids change the way the long chain is able to fold. This one change in primary structure ends up changing the secondary, tertiary, and quaternary levels of structure in the entire hERG potassium channel. Just like everything else in life, a change in structure is also a change in function. For SQT syndrome, this change results in a faster passage of potassium through the channel out of the cardiac cell - a gain of function - that makes the ventricles able to contract before they have enough time to fill with blood.
There seem to be multiple mutations between positions 35 and 36 on chromosome 7 that can cause LQT2. These mutations cause a loss of function in the hERG potassium channel, reducing the rate at which potassium can leave the cell. This makes the ventricles unable to contract when they should because they take too long getting back to their baseline potassium levels.
Saturday, January 9, 2010
Wednesday, January 6, 2010
Tuesday, January 5, 2010
Conversation Between Selves
You are best and brightest when you are happy for the triumph of a friend.
I see this in your photograph. You are holding the bouquet you caught.
You are best and brightest when you are listening to the pain of others.
I see it in their eyes. You make them believe they are strong.
You are best and brightest when you are taking enormous risks.
I see you hold the photograph up to your face. You are wondering if it is really you.
Monday, January 4, 2010
Dear Julie
Back in Bloomsburg and feeling much better than I ever expected. I am not alone - the Shrew is here with me, shrieking at me to keep carrying the fire, to keep absorbing and spewing truths. Here is a sensitive little project by Miranda July so you won't let me or anyone fade into the background.
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