100% satisfaction guarantee Immediately available after payment Both online and in PDF No strings attached
logo-home
WGU BIOCHEMISTRY 785 FINAL EXAM 100Q QUESTIONS WITH VERIFIED CORRECT ANSWERS/A+ GRADE 2023 VERSION $17.99   Add to cart

Exam (elaborations)

WGU BIOCHEMISTRY 785 FINAL EXAM 100Q QUESTIONS WITH VERIFIED CORRECT ANSWERS/A+ GRADE 2023 VERSION

 1 view  0 purchase
  • Course
  • Institution
  • Book

WGU BIOCHEMISTRY 785 FINAL EXAM 100Q QUESTIONS WITH VERIFIED CORRECT ANSWERS/A+ GRADE 2023 VERSION

Preview 3 out of 17  pages

  • November 2, 2024
  • 17
  • 2024/2025
  • Exam (elaborations)
  • Questions & answers
avatar-seller
WGU BIOCHEMISTRY 785 FINAL EXAM 100Q
QUESTIONS WITH VERIFIED CORRECT ANSWERS/A+
GRADE 2023 VERSION
What is the basic structure of an amino acid? What do they look like? - ANSWER:
amino group (NH2 or NH3), carboxyl group (COO or COOH), alpha carbon (C), and
variable group

How do you identify the 3 different types of side chains: non-polar/hydrophobic,
polar, and charged? - ANSWER: Non-polar/hydrophobic - end with CH or "can't have"
water. Polar - end with OH, SH, or NH. Charged - end with a charge

what kinds of bonds do each of the 3 different types of side chains make? - ANSWER:
ionic, hydrophobic/non-polar, charged

What are the 4 levels of protein structure? - ANSWER: Primary - linear structure,
Secondary - Folded into helix or pleated sheet caused by hydrogen bonding, tertiary -
3D structure caused by side chain interactions, quaternary - 1+ amino acid chains
combine = multiple subunits MUST have 1+ subunit

What enviormental change breaks each type of bond? - ANSWER: hydrophobic -
temperature change, ionic - salt or decreased pH, hydrogen - temperature, change in
pH, disulfide - reducing agents

what type of amino acid side chain leads to protein aggregration? - ANSWER:
hydrophobic bonds

how do environmental changes affect protein folding? - ANSWER: Extreme temp can
cause hydrogen bonds to break apart = malformation of protein folding

how do mutations affect protein structure? - ANSWER: Can cause structure to
change. Protein loses form = loses function. May form a different protein.

What is an electron? - ANSWER: Negatively charged atom on outer ring for bonding

What is energy: - ANSWER: Power derived fro chemical interaction

what are covalent bonds? - ANSWER: chemical bond, atoms share 1+ valence
electrons

what is an ionic bond? - ANSWER: bond between positive and negative

what is a hydrogen bond? - ANSWER: weak bond between positive and negative

with an amino? - ANSWER: piece of amino acid, NH2 or NH3

,what is a carboyxl? - ANSWER: piece of amino acid, COO or COOH

What is hydrophobic? - ANSWER: Doesn't like water, end with CH

what is hydrophilic? - ANSWER: Water Lovering, end with OH, NH, or SH

what is disulfide bond? - ANSWER: strongest bond between reduction agents,
formed between SH's.

what are zwitterions? - ANSWER: amino with positive and negative charges = overall
charge of zero

what is a polypeptide - ANSWER: polymer of amino acids

What is dehydration synthesis? - ANSWER: Process of forming peptide bonds

what is hydrolysis? - ANSWER: adding water to destroy bonds

what is an alpha helix? - ANSWER: twisted secondary structure, formed by hydrogen
bonds

what is a beta sheet? - ANSWER: folded second structure shape, formed by hydrogen
bonds

what is denaturation? - ANSWER: loss of shape duet o interruption of chemical
bonds; occurs via extreme salt, temp, pH

what is aggregation? - ANSWER: clumping of inner or outer cellular proteins caused
by misfolded proteins leading to diseases such as Alzheimers, ALS, Parkinson's

how do enzymes catalyze reactions? - ANSWER: bind with substrates to decrease
activation energy required and decrease reaction rate

how do enzymes affect reaction rate and activation energy? - ANSWER: decrease
activation energy and decrease reaction rate

what are the 4 steps of the enzymatic cycle? - ANSWER: enzyme recognizes
substrate, substrate attracts the enzyme; enzyme-substrate complex is formed;
enzyme-product complex formed; product is released, enzyme recycled

how do environmental changes affect enzymes? - ANSWER: High heat, pH change,
high salt concentration, and reducing agents can cause an enzyme to lose its
form/lose function

what is a competitive inhibitor? - ANSWER: Mimics substrate and takes its place on
the active binding site

, what is a noncompetitive inhibitor? - ANSWER: Binds to allosteric site causing active
site to change shape = preventing substrate from binding with enzyme

what molecules increase/build up or decrease given a specific inhibitor? A ->
(enzyme 1) -> B -> (enzyme 2) -> C -> (enzyme 3) -> D. Pretend Enzyme 2 is inhibited.
- ANSWER: Inhibitor would cause a build up for product B, decrease product C.
Enzyme 3 and product D would not be created.

what is substrate? - ANSWER: the substance on which an enzyme acts

what is a product? - ANSWER: result of a reaction

what is an intermediate? - ANSWER: products produced in an enzyme pathway
before final product

what is an active site? - ANSWER: location where substrate binds with enzyme

what is enzyme specificity? - ANSWER: Enzymes bind with certain substrate or type
of substrate to create a certain reaction

what is induced fit? - ANSWER: Enzyme changes shape in enzyme-substrate complex
to facilitate formation of enzyme-product complex

what is kinase? - ANSWER: Enzyme, adds phosphate group via phosphorlation

what is phosphatase? - ANSWER: enzyme, removes phosphate group via
dephosphorylation

with is an allosteric site? - ANSWER: secondary site on an enzyme an inhibitor binds
to via non-competitive inhibition

what is competitive inhibition? - ANSWER: enzyme substrate and inhibitor complex
compete to bind with enzyme's active site. no product formed when inhibitor binds
with enzyme.

what is non-competitive inhibition? - ANSWER: inhibitor binds to allosteric site, not
active site. Changes shape of active site, preventing substrate from binding and
making product

what is feedback inhibition? - ANSWER: End product sends feedback to beginning of
enzyme pathway inhibiting 1st enzyme via noncompetitive inhibition

what nucleotides/bases are used in DNA? what are their abbreviations/full names? -
ANSWER: C - cytosine, G - guanine, A - adenine, T - thyamine

what nucleotides/bases are used in RNA? - ANSWER: C - cytosine, G - guanine, U -
uracil, A - adenine

The benefits of buying summaries with Stuvia:

Guaranteed quality through customer reviews

Guaranteed quality through customer reviews

Stuvia customers have reviewed more than 700,000 summaries. This how you know that you are buying the best documents.

Quick and easy check-out

Quick and easy check-out

You can quickly pay through credit card or Stuvia-credit for the summaries. There is no membership needed.

Focus on what matters

Focus on what matters

Your fellow students write the study notes themselves, which is why the documents are always reliable and up-to-date. This ensures you quickly get to the core!

Frequently asked questions

What do I get when I buy this document?

You get a PDF, available immediately after your purchase. The purchased document is accessible anytime, anywhere and indefinitely through your profile.

Satisfaction guarantee: how does it work?

Our satisfaction guarantee ensures that you always find a study document that suits you well. You fill out a form, and our customer service team takes care of the rest.

Who am I buying these notes from?

Stuvia is a marketplace, so you are not buying this document from us, but from seller charitywairimuuu. Stuvia facilitates payment to the seller.

Will I be stuck with a subscription?

No, you only buy these notes for $17.99. You're not tied to anything after your purchase.

Can Stuvia be trusted?

4.6 stars on Google & Trustpilot (+1000 reviews)

75632 documents were sold in the last 30 days

Founded in 2010, the go-to place to buy study notes for 14 years now

Start selling
$17.99
  • (0)
  Add to cart