Brainscape's Knowledge GenomeTM

Browse over 1 million classes created by top students, professors, publishers, and experts.


See full index

tutto bio > ppt > Flashcards

ppt Flashcards

1
Q

Characteristics of living organisms:

1.
2.
3.
4.
5.
6.

A
  1. Consist of one or more cells
  2. Contain genetic information
  3. Use genetic information to reproduce
  4. Can convert molecules from their environment into new molecules
  5. Can extract energy from the environment to do biological work
  6. Regulate their internal environment
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

Cell Theory

A
  1. Basic structural and physiological unit of all life
  2. Cells come from cells
  3. Cell similar in chemical composition
  4. Most of chemical reactions of life occur within cells
  5. Sets of genetic information are replicated and passed on during cell division.
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

Eukaryotic cells evolved from
prokaryotes (endosymbiosis theory).

They have organelles.
Organelles—____ with specialized functions:
* nucleus
* chloroplast
* mitochondria

A

Membrane bound compartments

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

DNA: the information that is passed from __ to __cells.

Built of ____

Gene:

Mutations are ___ in the ____.

A

parent

daughter

repeating subunits–nucleotides

specific segment of DNA molecule, containing information for making proteins

alterations in the nucleotide sequence

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

Genome:

All cells in a multicellular organism
have ____.

A

all the nuclear DNA in the cell

the same genome

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

Living organisms interact:

– Individuals are part of ___.

Interacting populations of many different species form a ___.

Interacting communities in a given area form ___.

A

populations

community

ecosystems

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

Molecules in living organisms:

Most are ____.

A

proteins;
carbohydrates;
lipids;
nucleic acids

polymers formed by covalent
bonding of monomers

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

Polymers are formed by ___.

  • Protein monomers =
  • Carbohydrate monomers =
  • Nucleic acid monomers =
  • Lipids aren’t built of monomers but form ____.
A

covalent linkages of smaller units called monomers

amino acids

monosaccharides

nucleotides

large complexes considered as macromolecules

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

Reactions of Carbon compounds depend upon the presence of ___, each of which has ____ and ___ which it _____.

A

functional groups

specific chemical property

behavior

confers to the larger molecules

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

Six main functional groups:

__ = Hydroxyl – alcohols

__ = Carbonyl – aldehydes & ketones

__ = Carboxyl – acids

__ = amino – bases

__ = Phosphate - energy storage & transfer

__ = Sulfhydryl - cross links – similar to OH

A

-OH

-C=O

-COOH

-NH2

-PO4

-SH

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

Six main functional groups:

-OH =
-C=O =
-COOH =

-NH2 = amino – bases
-PO4 = Phosphate - energy storage & transfer
-SH = Sulfhydryl - cross links – similar to OH

A

Hydroxyl – alcohols

Carbonyl – aldehydes & ketones

Carboxyl – acids

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

Most biologic polymers are formed in ____. During which, _____.

These reactions require the following input:

A

condensation (dehydration synthesis) reactions

water molecule is removed

energy

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

Proteins have diverse structures & functions:

Proteins have important roles:
*
*
*
* Transport molecules
* Receptors
* Genetic regulatory molecules
* Structural units

A

enzymes
defensive molecules
hormonal/regulatory molecules

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

Proteins have diverse structures & functions:

Proteins have important roles:
* Enzymes
* Defensive molecules
* Hormonal/regulatory molecules
*
*
*
*

A

transport molecules
receptors
genetic regulatory molecules
structural units

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

Proteins made from ___.

  • Proteins range in size from a few amino acids to thousands.
  • Some proteins are composed of a single chain of amino acids, called a polypeptide. Other proteins
    have more than one polypeptide chain.
  • ___ is crucial to the function of a protein and is influenced largely by the sequence of amino
    acids.
  • Each different type of protein has a characteristic ___ composition and __.
A

20 different amino acid monomers

polypeptide

polypetide chain.

Folding

amino sequence acids

amino acid

order

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

Amino acid: protein’s building blocks

Due to the presence of the __and ___ group, amino acids are simultaneously acids and bases.

  • The amino group is the basic __
    part (__). The acid is a __group (__).
  • Differences in amino acids come from the __, attached to the
    ___ as the amino and the carboxyl
    group
A

amino

carboxyl

nitrogen containing

(H2N)

carboxyl

(COOH)

side chains (R-groups)

same carbon

17
Q

The α carbon is __because it is
bound to __ or __.
* Therefore, amino acids exist in two ___, __-amino acids and __- amino acids.
* Only __-amino acids commonly found in organisms.

A

asymmetrical

four different atoms

groups of atoms

isomeric forms

D

L

L

18
Q

Amino acids can be classified based on the characteristics of their ___.

A

R-groups

  • Charged hydrophilic side chains.
  • Polar but uncharged side chains.
  • Nonpolar hydrophobic side chains
19
Q

__ amino acids attract ions of opposite charges.

___amino acids with __ but
___ form hydrogen bonds

Hydrophobic amino acids; nonpolar hydrophic chains

A

hydrophilic

hydrophobic

polar

uncharged side chains

20
Q

Hydrophylic amino acids attract ___.

Hydrophylic amino acids with polar but uncharged side chains form ___

Hydrophobic amino acids; nonpolar hydrophic chains

A

ions of opposite charges

hydrogen bonds

21
Q

Amino acids with special properties
* __ has a terminal —SH group, which allows it to form disulfide bridges with other __ molecules.

  • __ has a hydrogen atom as the side chain. This makes it small enough to fit into small spaces and tight corners when the protein folds.
  • __ has a modified amino group that forms a covalent bond with the R group. The ring limits rotation of the carbon’s bond.

__ is often found at bends and loops of proteins.

A

Cysteine

Glycine

Proline

22
Q

Proteins are also called ___.
The first amino acid of a peptide is the ___ amino acid because the amino group is __ or __. The last amino acid of a peptide is the __ & has a __ group.

A

polypetides

N-terminus

free or unbound

C-terminus

free carboxyl

23
Q

Amino acids with special properties
* Cysteine has a terminal —SH group, allowing it to form disulfide bridges with other cysteine molecules.
* Glycine has a hydrogen atom as the side chain. This makes it small enough to fit into small spaces and tight corners when the protein folds.
* Proline has a modified amino group that forms a covalent bond with the R group. The ring limits __ of the carbon’s bond.

Proline is often found at bends and loops of proteins.

A

folds

rotation

24
Q

Primary Structure

Primary structure: the ___.
* It is determined by ___.
* It determines how, & where __ & __of the molecule may occur.

A

precise sequence of amino acids

covalent bonds

folding

bending

25
Q

A protein’s secondary structure consists of the __, __ patterns in different __ of the ___chain.

  • This shape is influenced primarily by __ arising from ___.
  • The two common secondary structures, are the ___ & ___.
A

regular

repeated

regions

polypetide

hydrogen bonds

primary structure

α helix

β pleated sheet

26
Q

Tertiary structure is the __
shape of the __, determined by
interactions among the __ of the amino acids.

  • The outer surface of the protein
    presents functional groups, which can interact with other molecules in the cell, such as other proteins or small molecules.
A

3-D shape

completed polypetide

side chains

27
Q

Quaternary structure results from
___ ___ing and __ing.

A

multiple polypetide SUBUNITS

binding

interacting

28
Q

Changes in __, __or high concentrations of __can change the __ of proteins. This loss of structure is called __.

A

temperature

PH

polar substances

3-D shape

structure

denaturation

29
Q

____ is the 3-D shape of the completed polypeptide, determined by interactions among the side chains of the amino acids.

  • The outer surface of the protein
    presents ___, which can interact with other __ in the cell, such as
    other proteins or small molecules.
A

Tertiary structure

functional groups

molecules

30
Q
A
31
Q

Six main functional groups:

A

tutto bio (7 decks)

Brainscape helps you reach your goals faster, through stronger study habits.
© 2024 Bold Learning Solutions. Terms and Conditions