Brainscape's Knowledge GenomeTM

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


See full index

Biochemistry and Mollecular Biology > Biochemistry Chapter 4 > Flashcards

Biochemistry Chapter 4 Flashcards

You may prefer our related Brainscape-certified flashcards:
AP® Biology flashcards Biology 101 flashcards
1
Q

Classification of proteins based on overall shape and protein, name the two kinds

A

Fibrous

Globular

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

Fibrous Protein

A

Elongated in shape, extracellular proteins and provides mechanical strength to cell and are insoluble in water

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

Globular protein

A

Globular proteins have more compact roundish shape, usually water soluble (eg many enzymes)

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

Examples of fibrous protein

A

Keratin (hair), myosin (connective tissue) tropomyosin,

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

What dictates how a protein will fold?

A

Chemical nature of side chain (is it polar or non polar) and the local environment (ie is it a polar or non polar solvent)

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

Examples of Polar solvent versus non polar

A

Polar: water. Non polar-Chloroform

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

Organization of proteins

A

Primary
Secondary
Tertiary
Quaternary (Not present in all proteins)

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

Primary Sequence (structure) of proteins

A

Dictates the secondary structure and All proteins have this

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

Secondary structure is the ____total of

A

All proteins have this, requires NMR and crystallography to determine

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

Tertiary Protein structure

A

All proteins have this, requires NMR and crystallography to determine

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

Quaternary structure

A

Only multi-subunit proteins have this structure

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

A multi-subunit protein with quaternary structures consists of

A

multiple polypeptide chains

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

Condensation reaction, to join two things…you have to remove

A

water

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

condensation reaction is also called the _____ reaction or _____synthesis

A

dehydration

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

Peptide bond, also called an _____ bond is formed between the a(- nitrogen atom of one amino acid and the carbonyl carbon of a second.

A

amide

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

Leucine has a hydro___ side chain

A

phobic

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

N-terminus is:

A

the end chain of the amino acid that is an Amino terminal residue (look for the NH3+ bond)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

C terminus is:

A

Carboxyl terminal residue (look for the C=OO bond

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

Peptide is a very _____ ____ amino acids

A

short sequence of 8-10

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

Protein chain or polypeptide chain, it is usually ___, or ___ or even ____ amino acids

A

100, 200 or 1000

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

_____ is the largest protein

A

Titin

22
Q

Titin

A

has a kinase domain for signaling and also functions mechanically as a molecular spring to provide muscle with elasticity, allow postcontraction recovery, and prevent overextension

23
Q

1 Dalton = weight of One ___ atom

A

Hydrogen

24
Q

Molecular weight of 1 amino acid= _____ g mol -1 which equals ____ Dalton.
1000 Dalton = ___kDa

A

110
110
1 (kilo Dalton)

25
Q

Different combinations of polypeptide chains formed = 20^n, where n is the number of ___ ___ involved in building a polypeptide chain

A

amino acids

26
Q

Linear polypeptide chain can be cross linked by _____ crosslinks

A

disulfide

27
Q

Oxidation to create a new bond results in a loss of ____

A

hydrogens

28
Q

Reduction of a chemical is the gaining of_____ to break apart the bond

A

hydrogens

29
Q

Cysteine is the ______ form, as ____ atoms are attached

A

Reduced

Hydrogen

30
Q

Cystine is the ______ form, due to the new bonding and loss of ____

A

Oxidized

Hydrogens

31
Q

Protein modification (Oxidation-reduction reactions) take place in the _____ _____

A

rough ER

32
Q

Inside the cell, the cytoplasm is very ___ so you will never have oxidation there, as oxidation would take place inside a compartment

A

Reducing

33
Q

You will never find ____ bonds in the soluble part of the cytoplasm

A

disulfide

34
Q

The first protein to be sequenced is___

A

insulin

35
Q

_____bonds help to modify protein and fold proteins so that it can function properly

A

Disulfide

36
Q

Protein ___ plays a major role in the function of a protein

A

modification

37
Q

Peptide bonds have _____ double bond characteristics that prevents ___ about the peptide bond. It is also uncharged, allowing formation of globular structures

A

partial

rotation

38
Q

Peptide bonds are:

  • Planner
  • ____
  • Partial double bond characteristics
  • Very rigid
A

Uncharged

39
Q

Peptide bonds in proteins are almost always _____, as steric hindrance would prevent it from being cys as the side chains of the amino acids can be very bulky

A

trans

40
Q

Bond between the alpha carbon and the Nitrogen (amino) is the ____

A

phi (a circle with a line through it)

41
Q

Bond between the alpha carbon and the Carbon (carbonyl) group is the ___

A

Psi (Looks like a cactus or a trident)

42
Q

If the rotation is in a clockwise rotation it is represented by a ____ value. and if it is rotating in an anti clockwise rotation it is represented by a ____ value

A

Positive (+)

negative (-)

43
Q

Hydrogen bonding scheme for Alpha Helix formula is: Carbonyl group of amino acid (n) forms Hydrogen- bond with NH(Amino) group on the (n + ___) amino acid on the ____ strand. Only one strand is involved in Alpha Helix!

A

4th

SAME

44
Q

If you see a rod shaped protein chain, it is called an _____ _____

A

alpha helix

45
Q

Valine, Threonine and isoleucine can not be in an alpha helix due to _____at the beta carbon

A

branching

46
Q

Serine, Aspartate and asparagine can not be in an alpha helix due to side chains containing ____ donors and acceptors very close to the main chain

A

Hydrogen

47
Q

Proline can not be in an alpha helix as it lacks an NH group and ____ alpha helix. It has a ____ ring structure and cannot assume the phi value to fit into a helix

A

breaks

rigid

48
Q

Due to Prolines rigid ring like structure, nature uses Proline to form a ____ in the structure of a protein

A

bend/fold

49
Q

Determining direction of helix, look at if the “screw”and ______ from the top, is it going clockwise or anti-clockwise.

A

tracing

50
Q

Alpha helix that are ____ handed are more common

A

right

Biochemistry and Mollecular Biology (6 decks)

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