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UW Madison Bio 101 Exam 1 Questions & Answers(GRADED A+).
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UW Madison Bio 101 Exam 1 Questions & Answers(GRADED A+). UW Madison Bio 101 Exam 1 Questions & Answers(GRADED A+).

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  • October 21, 2024
  • 16
  • 2024/2025
  • Exam (elaborations)
  • Questions & answers

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  • uw madison bio 101 exam 1 questions answersgrad

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UW Madison Bio 101 Exam 1
Questions &
Answers(GRADED A+)
✅✅
Basic research- Driven by basic interests in a subject.
Applied research- designed to solve practical problems - -Difference
between applied research and basic research

order- everything has order, regulation- everything has to have some
control, growth and development- we all grow and develop as life goes on,
energy processing- we all process energy to survive, response to the
environment- we adapt to where we are and what we do, reproduction-

✅✅
goal of life is to produce more, evolution- overtime we change to live better
- -What are the properties of life?


✅✅
Molecule, organelle, cell, tissue, organ, organ system, organism,
population, community, ecosystem, biosphere - -List the levels of
biological organization in order


✅✅
Least complex- Molecule
Most complex- Biosphere - -What level of biological organization is
least complex? Most complex?


✅✅
Characteristics that depend on a specific level of organization. Arise to
better suit environment - -What are emergent properties?


✅✅
All living things are made up of cells. Cells also exhibit all the
characteristics of life - -Why is the cell the basic unit of life?


✅✅
Bacteria and Archaea (prokaryotic- no nucleus, unicellular), Eukarya (true
nucleus, mostly multicellular) - -Three domains of life

Plants, animals, fungi, and protists. All are multicellular and most have

✅✅
tissues. Animals don't have cell wall, other all do. Plants- cellulose, Fungi-
chitin, Protists- varies. - -Compare and contrast eukaryotic kingdoms
of life

A family tree that shows the evolutionary relationships thought to exist

, ✅✅
Partial charges attract. Partial positive charge on hydrogen is attracted to
the partial negative charge on oxygen. - -How does the structure of
water lead to hydrogen bond formation?

O-H, N-H, S-H - ✅✅-Polar covalent bonds important in biological
structures:

Salt dissolves in water due to the salt molecule being a charged molecule
(ion). Partial charges in water are attracted to charged particles in salt. Oil

✅✅
does not dissolve in water because oil is non-polar meaning it has no
electrons to share with water. - -Why does salt dissolve in water?
Why doesn't oil?

Hydrolysis- Addition of water to break apart molecule

✅✅
Dehydration synthesis- The process of removing water to build a monomer.
- -Hydrolysis vs Dehydration synthesis

monosaccharides- single sugar (glucose for example)
Disaccharide- two sugars put together

✅✅
Oligosaccharide- 3-10 monosaccharides put together -
-monosaccharides vs disaccharides and oligosaccharides

Starch, Glycogen, Cellulose, and Chitin. All made up of glucose
monosaccharides put together.
Starch- used in plants for energy storage
Glycogen- used in animals and fungi for energy storage

✅✅
Cellulose- found in plants, used to help keep plant upright
Chitin- structural support in fungi - -Four major polysaccharides;
structure and function

Due to an enzyme that allows them to break down cellulose - ✅✅-Why
can't humans digest cellulose? But cows can


✅✅
dehydration synthesis, peptide bonds link amino acids in the primary
structure of a polypeptide - -How are peptide bonds formed? What do
peptide bonds do?

Primary- Linked series of amino acids w/ unique sequence.
Secondary- Localized folding created by H-bonding. Interactions between
non-R groups. Alpha helix and beta pleated sheet.

, 1. H-bonding
2. Covalent bond: disulfide bridge s-s
3. Ionic bonds (charged particles)

✅✅
4. Hydrophobic exclusion, molecules huddled inside of protein -
-Types of interactions between R-groups in tertiary structures

1. Substrate enters active site of an enzyme
2. Induced fit
3. Substrates converted to products
4. Products are released

✅✅
5. enzyme returns to its original tertiary structure and can bind another
substrate molecule - -How an enzyme works:

If an amino acid is changed in primary structure of a protein sequence, this
could happen:
always changes primary structure
Sometimes changes secondary structure of protein

✅✅
Can affect protein function
Can sometimes change tertiary structure of a protein - -Things that
affect protein function

Temperature- higher temps cause denaturation of proteins. Lower temps
slow down activity of protein.
pH:

✅✅
-higher H+= more acidic,
-higher OH-= basic - -Things in the environment that can lead to
denaturation of proteins and function

Hormones
Membrane structure

✅✅-Function
Four ring structure is always steroid
Reduce production of chemicals that cause inflammation -
of steroids in human body

Saturated- Straight chains (single bonds), animals fats, packed tightly, solid
at room temp. Raise levels of HDL and LDL in blood=bad
Unsaturated- Curved chains (double bonds), plants and oils, loosely

✅✅
packed, liquid at room temp. Lower LDL and raise HDL=good -
-Saturated vs Unsaturated fats

LDL- carries cholesterol from liver through bloodstream to body cells.

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