BIOS 1705 Lecture 4: BIOS 1700 Lecture and Book Notes #3 PDF

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silvergerbil790

5 Sep 2016

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Key organic molecules in the cell: hydrophilic (water-loving) molecules; rich in polar covalent bonds. Simple sugars (monomers) and carbohydrates (polymers: monomers are the building blocks of the chains, polymers are the chains, hydrophobic (water-fearing) molecules; rich in non-polar covalent bonds. Dna nucleotide structure: a phosphodiester bond is between the oh of one nucleotide and the oh of the nucleotide next to it. In the process water is released: there are two classes of nitrogenous bases: Pyrimidine (smaller: thymine (t, cytosine (c, uracil (u) Purine (bigger: adenine (a, guanine (g, base pairs are complementary. So in dna adenine is paired with thymine and guanine is paired with cytosine. In other words, a always equals t and g always equals c. In rna, adenine is paired with uracil. A always equals u and g always equals c: the bond between a and t only has 2 hydrogen bonds and is weaker than the g and c bond which has 3 hydrogen bonds.

Related Questions

For each of the following sentences, fill in the blanks with the best word or phrase selected from the list below. Not all words or phrases will be used; each word or phrase should be used only once. Proteins are ______________ built from amino acids, which each have an amino group and a _____________ group attached to the central _______________. There are twenty possible _______________ that differ in structure and are generally referred to as âR.â In solutions of neutral pH, amino acids are _______________, carrying both a positive and negative charge. When a protein is made, amino acids are linked together through _______________, which are formed by condensation reactions between the carboxyl end of the last amino acid and the ___________________ end of the next amino acid to be added to the growing chain.

a: amino	b: ionized	c: polypeptides
d: alpha-carbon	e: length	f: protein
g: carbon	h: noncovalent	i: R group
j: carboxyl	k: peptide bonds	l: side chains

m: hydroxide

indigofrog836

1. Polypeptide strands is the active form of a digestive enzyme in the stomach that breaks polypeptide chains into smaller polypeptides.

2. Cleavage of proteins by pepsin in the stomach results in formation of pepsinogen which get broken down further in the small intestine.

3. An amino acid chain made up of three amino acids joined together is called a tripeptide.

4. Dipeptide describes an amino acid chain made up of two amino acids joined together.

5. The 20 different amino acids are the building blocks used for protein synthesis.

6. Amino acid pools are stockpiles found in the blood and other cells of the body that can be used to build new proteins.

7. The continual process of degrading and synthesizing protein is called protein turnover.

8. The stomach produces pepsin, which denatures protein.

9. Denaturation occurs when a protein is exposed to heat, acid, bases, or mechanical agitation resulting in unfolding of the protein, though the peptide bonds remain intact.

10. The part of an amino acid that contains nitrogen is called the amine group.

11. The acid group is also known as the carboxyl group.

12. Single amino acids that are absorbed in the small intestine travel to the liver via the portal vein.

Please correct these sentences AS SOON AS POSSIBLE.. Some of them are not correct and I didn't figure out what are they!

violetdog828

Is DNA a protein if so what makes up proteins, if not what it is and what are its monomers called? Describe the primary, secondary, tertiary, and quaternary structure of DNA (this sub-question is independent of the answer to the first question).

Describe electrostatic bonds, covalent bonds, van der Waals interactions, and hydrogen bonds and give an example of each.

Which of the four classes of amino acids has side chains with the greatest hydrogen-bond-forming potential?

Which has the greatest potential to form electrostatic interactions?

Which class has the greatest potential for hydrophobic interactions?

Of the following amino acids, (K), (Y), and (F), which side-chains would you expect to be the most soluble in a polar aqueous solution? Which the least?

Would you agree with the statement that many different amino acid sequences can fold into the same basic tertiary structure? What data can you cite as evidence for your position?

BIOS 1705 Lecture 4: BIOS 1700 Lecture and Book Notes #3 PDF

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