BIOB10H3 Lecture Notes - Lecture 2: Globular Protein, Protein Domain, Intramolecular Force

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2 Feb 2019

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If there is amino acid that like another amino acid, they from secondary structure, the alpha one and beta. All proteins might do this naturally and fold or some cant fold on its own so the chaperones will come and help them. Tertiary has two types long fibers and globular protein. The distance bonds will from a non covalent bond to stabilize this. After translation is cleaving, sugar added, metal. ion added. There is lots of enzymes that are destructive. It interacts with negative dna with amino acid that is positive that portion would be dna binding protein. It allows protein activity, it is parts of the tertiary structure that have a function. Only some proteins will do this if there tertiary structures tells it to. It can be a host of lots of bonds. Two tertiary structures come together to make a quaternary structure. This is a small protein. it is discovered by banting and best nobel prize in 1923.

Related Questions

1. What is an organic molecule?

2.Name three hydrocarbons and be able to draw their structural formulas.

3. What is an isomer? List and describe the three types (structural, geometric, and enantiomers).

4. Be able to recognize and describe the properties of these functional groups: aldehyde, ketone, hydroxyl, sulfhydryl, carboxyl, amino, and phosphate groups.

5. What is a monosaccharide? Give two examples of these molecules and their functions.

6. Describe these chemical reactions: dehydration synthesis (condensation reaction) and hydrolysis (rehydration).

7. What is a disaccharide? List two and give their functions.

8. What is a polysaccharide? List two storage forms and two structural forms. How are they formed and what is their specific function?

9. How do the pancreatic hormones insulin and glucagon regulate blood sugar levels?

10. What is molting and why is it necessary in certain animals?

11. What four molecules are bonded together to form a triglyceride or fat? Why are fats nonpolar? What are some functions of fats as well as other lipids such as oils and waxes?

12. How do saturated and unsaturated fats differ? Discuss bonding patterns and possible sources of these fats. Which type is healthier for you? Why?

13. Why do animals store most of their excess glucose as fats or oils rather than as glycogen or protein? Give two reasons.

14. What are phospholipids? Identify parts of the phospholipid bilayer that are hydrophobic or hydrophilic? What important cell structure do these molecules help create?

15. Describe the structure of a steroid. How is cholesterol used in beneficial ways in your body?

16. What are LDLs and HDLs? Which is considered good or bad cholesterol? What condition could result from high blood pressure?

17. What are four ways to either reduce high blood cholesterol or maintain a safe level?

18. What is the composition of an amino acid? Why would they be considered nonpolar, polar, acidic, or basic?

19. Define dipeptides and polypeptides.

20. Describe the primary structure of a protein. What type of bonding creates it?

21. What is the secondary structure of a protein? Name two types of secondary structure and indicate what type of bonding holds them together. List three fibrous proteins.

22. What is the tertiary structure of a protein? What types of bonds or chemical interactions allow a protein to maintain this structure? List three globular proteins.

23. What is the quaternary structure of a protein? Describe a hemoglobin molecule.

24. What are the subunits of nucleic acids and what is their composition? How are these subunits bonded together? What is DNS's basic shape?

25. List three differences between DNA and RNA.

After working through the macromolecules in your friendâs extremely pale burrito, you look at her and think you might have an idea about what is going on. You ask Maria, âDo you usually eat like this?â âYup,â she says, âI love all the carbs, rice, and bread, as well as cheese. Sometimes I eat a piece of fruit or some carrot sticks. And energy drinks!â You then point out to your friend that she seems to be getting very little protein, a major class of macromolecules. But she is getting plenty of carbohydrates and lipids in the form of animal fats.

1. While your body can convert the monomers of macromolecules from one to the other, it has to have the raw materials in the form of the appropriate atoms. You explain to your friend that when she eats proteins, they are broken down into amino acids through the process of INSERT ANSWER and can then be rebuilt into new proteins through the process of INSERT ANSWER.

a. If your body does not take in protein, but only carbohydrates and lipids, what atoms will it be missing? Hint: There are two, and you can figure this out by comparing the structures of the monomers for proteins and carbohydrates as well as the basic structure of lipids. INSERT ANSWER

b. For the above atoms, how many electrons are in the outer shell? INSERT ANSWER

c. For the above atoms, what type of bond will they make within the amino acid monomer? INSERT ANSWER

d. Even if your friend does obtain the correct atoms, there are still a couple amino acids that your body cannot manufacture from scratch, but must be ingested. What are these amino acids? INSERT ANSWER

e.Why might a lack of protein or the wrong types of proteins lead to your friendâs fatigue? INSERT ANSWER

The bacterium E. coli, which is a major model system for the study of genes and DNA, has a singular circular chromosome of about 4x106 bp. In contrast, human diploid cells have __1__ chromosomes, of __2__ different types (donât forget that the X Â¹ Y!). The total amount of DNA found in a haploid cell such as a sperm or egg is called the organismâs âC-valueâ; the human C-value is __3__.

Also in contrast to the E. coli circular chromosome is the fact that eukaryotic chromosomes are not circular, but instead are __4__. Eukaryotic chromosomes are complexed heavily with protein to form a DNA-protein complex generically called __5__. The proteins found can be considered to fall into two general classes: __6__ and __7__. The first class is made up of 5 major proteins called __8__, __9__, __10__, __11__, and __12__. On a weight to weight basis, these proteins make up about __13__% of the total mass of a chromosome. Since these proteins must associate relatively non-specifically with DNA, they are rich in the basic amino acids __13__ and __14__, which gives the proteins a net __15__ charge.

One goal of packaging the DNA into chromatin is to compact the genome so it will fit into a nucleus. The basic unit of chromatin structure is the __16__, which has __17__ base pairs of DNA wrapped around a âcore particleâ composed of __18__ copies each of the core histones. Each nucleosome is separated by a stretch of âlinkerâ DNA so that the repeating unit is approximately 200 bp. Lets do a little arithmetic: If we consider that the nucleosome is approximately __19__ nm in diameter, that there is about 200 bp in this structure, and that 200 bp of DNA would normally occupy __20__ nm if stretched out straight (recall that each base is spaced about 0.34 nm from the next), we can see that the nucleosome alone allows for a __21__-fold compaction ratio.

The nucleosome structure is further compacted by histone __22__, which is not a part of the core particle. Instead, this histone __23__ (does what?) to cause the nucleosomal 10 nm fiber to condense into a higher-order structure referred to as the __24__ nm fiber. In the nucleus, chromosomes do not just float around freely: they are tethered to a proteinaceous structure called the __25__ at specific DNA regions called âSARsâ, which stands for __26__. SARs are rich in topoisomerases, to allow the winding and unwinding of the DNA that accompanies replication and transcription to occur, despite this constraint.

The 30 nm fiber discussed above is the form in which transcriptionally active DNA is believed to exist in the nucleus; however, further condensation leads to a highly condensed inactive form called __27__; in this terminology, the active form is referred to as __28__. The inactive condensed form can be divided into two types: one type is essentially invariant between cell types, and since it is âon all t timeâ, it is referred to as __29__. The other type comes and goes, depending on the expression of the genes present in that region of the chromosome; it is referred to as __30__.

Eukaryotic chromosomes carry the genes, of course, but also have other functional regions. One such region is the place where the spindle apparatus attaches during mitosis and meiosis; this region of the chromosome is called the __31__. Another important part of the linear eukaryotic chromosome is the ends; these are called __32__. In humans, the end of each chromosome is composed of many repeats of the short sequence __33__. One more type of functional region on each chromosome is the place where DNA replication starts; in humans, each chromosome has several of these __34__. Thus, eukaryotic chromosomes carry several different types of functional sequences, which together allow for their __35__ during S phase, __36__ during mitosis and meiosis, and the __37__ of their genes

BIOB10H3 Lecture Notes - Lecture 2: Globular Protein, Protein Domain, Intramolecular Force

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