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~*~Surviving AP Biology~*~


Hey Ms. Pinder :)! This is my (Chad) AP Biology Journal, in the form of a Tumblr blog. This blog will consist of careers in biology, questions that i found the answer to, or just cool things i found on biology! Ask Me Anything Theme
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1 month ago   1 note   Reblog
A veterinarian, also known as a vet, is a doctor for animals and a practitioner of veterinary medicine. It is a solid and very stable career.The average veterinarian salary is between $70,000 to $90,000 annually. This is for vets that do not own their own practices. If you end up owning your own practice, the salary range increases to $100,000 to $250,000 and up per year.To become a Veterinarian, you must complete a degree in Veterinary Medicine and obtain a license to practice. Getting into veterinary school is very competitive.You must  graduate with a Doctor of Veterinary Medicine (D.V.M. or V.M.D.) degree in the United States. There are currently 28 schools that will provide this. Most schools do not require a full 4 year degree to enroll. Most will take 60 to 90 college hours as a perquisite. However, it is still better to have a bachelor degree as you have a better chance of being admitted with one.Generally, most veterinarians will end up in private practice operating their own business or joining into a partnership. However, you can also end up in an animal shelter, research center or zoo.
7 months ago   0 notes   Reblog
7 months ago   7 notes   Reblog
cognized: Cholesterol molecules look suspiciously like shrimp tempura. Yeah, that sounds about right.
7 months ago   34 notes   Reblog
hypocritesaint: in addition to eating, i’m taking amino acids (and other nutrients) as supplements to enchance mental and physical performance and to get a somewhat better results from training. they seem to help noticably, for me it might be cause of the poor diet i’ve had through out my life. but now days i think almost everyone has a poor diet and that effects the mind and body in many different ways. even anxiety and deppression can start just cause of a poor diet : ) alc, tryptophan, tyrosine, ornithine, lysine, arginine, creatine, taurine, omega-3 =)
8 months ago   26 notes   Reblog

oh baby.: Proteins: Structure and Function

sopebar:

proteins are macromolecules made up of amino acids

amino acids: building blocks of life, made up of

  • amino group
  • carboxyl group
  • hydrogen atom
  • R-group side chain (polar has O or S and is hydrophilic; charged has a charge and is hydrophilic; nonpolar has neither O/S nor charge, can tell by…
8 months ago   19 notes   Reblog

Amino Acids

buildingblocksoflife:

There are 20 amino acids that are the building blocks of protein primary structure.

Each has a long name, a three letter abbreviation, and a one letter abbreviation. 

Amino Acids link up the backbone amines to backbone carboxylic acids through condensation to form an Amide Bond

8 months ago   9 notes   Reblog
physiciantobe: Proteins are the most changing molecules in our body. They can have a structural function (es. collagen), serve as a catalyst in bioreactions (enzymes), work as carrier for many kind of molecules, act as antibodies, etc. Enzymes are really important: those proteins work as a catalyst in pretty much every reaction that occurs in living things. A catalyst is a substance that, when added to some reagents in a reaction, can highly accelerate the process by decreasing the peak of energy (activation energy, Ea) the solution has to reach before reagents (x,y) are transformed into products (z).  Without enzymes a lot of reactions would be really slow, unfit for life; at the other hand a lot of reactions wouldn’t occur, because enzymes may match more reactions, so that one in which energy is produced, may be used to “charge” the other one that needs energy to occur (we said that in nature this kind of reactions don’t naturally occur, idd). This is due to their particular conformation; enzymes got specific parts of the molecule called “catalytic site”, where reagents (substrate) take place and react, aided by the comfy spot in which they immediately fit in; otherwise, reagents molecules would need to crush accidentally, and this is statistically much less likely without enzymes. Enzymes can also be activated or deactivated by other molecules, activator or inhibitor, that can turn on or off an enzyme, enhancing or blocking it. This is how, i.e., some drugs or venoms work, and it’s called “allosteric modulation”. There’s also a modification called “covalent”; enzymes are regulated by a modification of their structure that has once again the effect of turning them on or off.
8 months ago   Notes   Reblog

“If I were an enzyme, I’d be DNA Helicase so I could unzip your genes.”

(Source: keepcalm-and-killzombies)

8 months ago   34 notes   Reblog
medicaljourney: I wanted to do a post on something we talked about in my Molecular and Cell Biology class - allosteric regulation and the use of allosteric sites in pharmacology. Allosteric regulation is essentially the regulation of an enzyme by binding a molecule (called an effector) at the enzyme’s allosteric site (a site other than the active site). I won’t jump right in and start talking about the use of allosteric sites as drug targets because it’s difficult to understand without talking about enzymes first. I’m going to go over some of the basics about enzymes for my readers who aren’t familiar with this. This is something we learned in Bio 202. Most chemical reactions in a physiological context, such as those occurring in a biological cell, need enzymes to occur at a sufficient rate in order to support life. In addition, enzymes are involved in the regulation of metabolism inside cells and the enzymes found in a cell determine which metabolic pathways occur in that particular cell. As most of you probably know, enzymes are proteins that increase the rate of chemical reactions. Enzymes catalyze reactions by lowering the activation energy, the initial energy needed to start a chemical reaction. The reactant that an enzyme acts on is called the substrate.  The enzyme binds to its substrate, forming an enzyme-substrate complex. Ultimately substrates are converted into different molecules, called products. The region on the enzyme where the substrate binds is the active site. The active site can lower the activation energy by orienting substrates correctly, straining substrate bonds, providing a favorable microenvironment or covalently bonding to the substrate. In addition, catalysis in the enzyme’s active site can be acid-base catalysis, in which enzyme side chains transfer protons to or from the substrate and a covalent bond breaks; covalent catalysis in which a functional group in a side chain bonds covalently with the substrate; or metal ion catalysis in which metals on side chains loose or gain electrons. One of the reasons why we need vitamins and minerals is because some enzymes require additional molecules for proper enzymatic function. They can be cofactors, which are metal ions (minerals), non-protein enzyme “helpers” that are found in the active site and participate in catalysis. Two examples are zinc and manganese, which destabilize bonds by drawing on electrons. Some enzymes may also require coenzymes, which are non-protein organic molecules, such as vitamins B2 (flavin) and B3 (niacin), which “store” energy containing electrons.   Enzymes fold into complex and specific 3D shapes that allow them to interact with their substrate and catalyze chemical reactions. However, most enzymes are regulated during metabolic activity, that is, they’re not all active at all times. In addition to the active site where the substrate binds, enzymes also have allosteric sites; sites where activators or inhibitors can bind. Activators and inhibitors stabilize enzymes in shapes where their active site is either accessible to the substrate (activator) or inaccessible to the substrate (inhibitor). Enzymes have a number of 3D conformations, in some their active site is exposed and available to substrates and in others their active sites are obscured or inaccessible. You can think of an enzyme as a protein that’s folding in a 3D shape and constantly going back and forth between different 3D shapes, waiting for activators or inhibitors to lock them into either the “on” or “off” state. Sometimes this means that the enzyme exists in a quaternary structure, meaning there is one protein subunit that has the catalytic activity (the ability to bind the substrate and promote the chemical reaction), but in addition there is another protein that attaches onto it and that is the regulatory subunit. The interaction between the regulatory subunit and the catalytic subunit effects the 3D conformation of the enzyme. The regulatory subunit has pockets where allosteric activators or inhibitors can bind. Enzyme inhibitors can be either competitive or non-competitive (allosteric). Competitive inhibitors are structurally similar to the substrate and they bind to the active site of an enzyme, competing with the substrate. Competitive inhibitors need to be in higher concentration than the substrate in order to work. Allosteric regulators are attractive drug candidates for enzyme regulation. Pharmaceutical companies like to use allosteric activators and inhibitors to target enzymes because in contrast to competitive inhibitors, whose effectiveness depends on the concentration of substrate, allosteric inhibitors bind to a site that is distinct from the active site so they are not affected by fluctuations in substrate concentration.   When someone is taking a medication, the pharmacokinetics of that medication are very important, i.e. when someone takes a pill, how long does it take for it to get into the blood stream? How many cells are going to take it in and how long will it be there in that form before the cell breaks it down? If a drug has to be present at a very high concentration because it’s competing with the substrate, it is going to be more problematic than something that is binding to the allosteric site. Particularly if you can develop a drug that binds to an allosteric site and covalently attaches itself there and permanently inhibits the enzyme. An example of this is pharmaceutical companies looking for an allosteric inhibitor of a caspase. Caspases are proteases, they are enzymes that cut proteins in specific places after particular amino acids, and they only cut certain proteins. When a caspase acts on its substrate, it activates it. This may seem counter initiative because if a protease cuts a protein, if it breaks a peptide bond, how could that make the protein more active? As it turns out, the targets of caspases are proteins that are made in an inactive form that need to be activated. If you have a protein that is an enzyme, but part of the protein, say the first few amino acids, are wedged into the active site of the enzyme, then these proteins have an auto-inhibitory subunit, they are made in an inactive form. A caspase comes along and cleaves off the auto-inhibitory part of it and activates it. There are many examples in human physiology where the activation of a caspase triggers the digestion of these auto-inhibitory components and activates cascades. For example, the blood-cutting cascade, apoptosis and the inflammatory response all involve the activation of caspases.   Caspases activate the activity of inflammatory cytokines, which promote the inflammatory response. There are many conditions that are the result of an inappropriate or overactive inflammatory response, such as arthritis and regional enteritis (crohn’s disease). A pill that inhibits the caspase, so that this enzyme stays in its inactive state and the inflammatory response cannot go forward, could help individuals manage these chronic inflammatory diseases. One such drug discovery experiment involved the collaboration of a pharmaceutical company and an academic lab. They knew that this enzyme caspase 1 had this allosteric site and that near the allosteric site was an amino acid containing a sulfur group, a cysteine or a methionine. They sought to find a molecule that would wedge into this site and form a covalent bond with that sulfur, effectively locking the enzyme in its allosterically inhibited confirmation so it could no longer trigger this inflammatory cascade. They screened several thousand molecules and came up with one that fit in the allosteric site and formed a disulfide bond, making those enzyme molecules inactive.  They could then make a medication that is taken daily to shut down this caspase, effectively helping to manage the inappropriate inflammatory response. Another example of a drug that allosterically regulates is the HIV treatment drug Maraviroc. This is a drug design philosophy, trying to discover molecules that can insert themselves in an allosteric site, covalently bond and shut down that enzyme at least temporarily.  
8 months ago   21 notes   Reblog
72000nadinavigator: Watermelon is good for high blood pressure, diabetes, poor eyesight, prevents heat strokes, cancer and impotence:) # yay fruit
8 months ago   26 notes   Reblog

This biology homework makes no sense at all. Like seriously, she wants this by tomorrow?

runaway-hearts:

(Source: dreamingskies)

8 months ago   26 notes   Reblog
8 months ago   7 notes   Reblog
glycolysisandall: The image above shows an example of an amphiphile which is a term used to describe a chemical compound that contains both lipophilic (fat-loving) and hydrophilic (water-loving) properties. A common and important class of amphiphillic molecules include phospholipids, which are the main component of cell membranes. The amphiphillic nature of these molecules actually defines the way in which the cell membrane is arranged. The arrangement of polar hydrophilic groups on the outside, so as to interact with the aqueous environment and non-polar lipophilic groups on the inside, away from the aqueous environment, hence forms the basis of the bilayer. 
8 months ago   32 notes   Reblog
8 months ago   1,386 notes   Reblog