Brainscape's Knowledge GenomeTM

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


See full index

Physics > Biochem thermo > Flashcards

Biochem thermo Flashcards

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

Primary source of protein stability

A

Hydrophobic interactions (H bond v important structural elements)

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

Entropic forces involved in dimerization

A

Conformational entropy (freedom to move) +, hydrophobic effect and hydrogen bonding (-)

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

What is ionization process influenced by

A

Special structural features of the protein (G intrinsic)
The charge of the protein created by other ionizable groups (G interaction)

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

Ways to unfold a protein

A

Temperature, pH, chemical denaturant (acid, base, urea), enzyme

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

Most common method for protein unfolding monitoring

A

Circular dichroism (abs spectroscopy method in the UV).

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

What forces are at play in base stacking

A

pi electron interactions and hydrophobic interactions (water is most favorable solvent for stacking)

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

Do all base pairs melt at same temp

A

No, AT has 2 bonds, GC 3
AT melts at lower temperatures

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

What is RNA

A

A linear polymer made of four different types of nucleotide subunits linked together by phosphodiester bonds with several biological functions

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

What is ELISA

A

The Enzyme-linked immunosorbent assay to quantify biological substances such as protein, antibodies, and hormones.

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

PCR def

A

The Polymerase Chain Reaction molecular biological technique (to produce thousands to millions of copies of a particular DNA fragment).

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

DNA rep

A

The biological process responsible for the synthesis of two identical copies of DNA from one copy.

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

Steps in DNA replication

A

Initiation
Elongation
Termination

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

Hess’s Law

A

the heat absorbed or evolved in a given reaction must always be constant
and independent of the manner in which the reaction takes place

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

Standard-state free energy of formation

A

change in free energy that occurs when a compound is formed from its elements in their most thermodynamically stable states at standard-state conditions

(difference between free energy of a substance and the free energies of its constituents at standard-state conditions)

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

Standard state conditions

A

1 M, 1 atm, 298 K, pH = 7

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

Exergy

A

available energy to do work

State-condition

System in equilibrium with environment -> exergy = 0 (no useful work can be obtained)

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

Catabolic reactions

A

Breakdown complex and higher E molecules into smaller ones
Release free E

Can be used to drive less favorable reactions

18
Q

Anabolic reactions

A

Energy consumed to build complex molecules (take up free E)
Ex: synthesis of proteins

19
Q

How can an unfavorable rxn be coupled with a favorable one

A

Enzymes directly couple energetically favorable rxns which release E and produce heat to unfavorable ones which produce biological order

20
Q

Enzyme

A

Protein that facilitates cellular metabolic processes by lower the activation energy levels to catalyze the chem rxns between biomolecules

21
Q

Activated carriers

A

Store E in easily exchangeable form as transferable chemical groups or electron at high E

They can be a source of E and chemical groups in biosynthetic reactions

-> coenzymes (ATP, NADH, NADPH)

22
Q

Phosphorylation of glucose by ATP

A

Phosphoryl group (PO32-) transfered from ATP to glu
Catalyzed by hexokinase
Unfavorable
Uses ATP ( -> ADP highly favorable rxn that releases E)

23
Q

Hydrolysis of ATP

A

ATP -> ADP highly favorable rxn that releases E

24
Q

Metabolic cycles

A

Metabolism = many sets of reaction to produce v specific molecules

rxns are coupled in that the product of one rxn = the reactant for the next reaction in the cycle

25
Q

Anaerobic glycolysis

A

Metabolic pathway that metabolizes glucose into lactate and produces ATP when limited O2 available

26
Q

Ionic strength

A

measure of salt concentration including all the ions present in a solution

27
Q

Membrane potential

A

Produces favorable gibbs energy for transport of K+ and unfavorable for transport of Na+

Membrane more permeable to K+ than to Na+

28
Q

Proteins

A

one or more polypeptide chain consisting of amino acids (side chains polar or nonpolar) whose sequence is coded from DNA

29
Q

Non polar groups of proteins

A

AA side chains containing methylene and methyl groups and aromatic residues

30
Q

Why does dissolving non polar protein in water correspond to positive gibbs

A

Enthalpy change is favorable but negative entropy change

Normal water structure broken apart, ice-like structures form around HC, decreasing disorder

31
Q

Zwitterion

A

positive and negative charges in the same molecule

32
Q

Hydrophobicity of protein

A

Non-polar side chains prefer nonaqueous environment, so they aggregate in the interior of the protein

33
Q

Ionization entropy source

A

Negative entropy due to ordering of the water molecules around the ions

Thermally neutral (enthalpy changes related to solvation of ions = enthalpic change due to breaking oxygen-hydrogen bonds)

34
Q

How do charged groups influence structure (pH)

A

High pH : negative charge interactions cause native structure to disappear

Low pH: positive charge interactions cause disruption of native structure

Salt linkage between opposite charge groups stabilize structure

35
Q

What is positive entropy and enthalpy due to in ionization

A

Positive entropy is due to the release of water of hydration of the ions when the ion pair is formed

Positive enthalpy is a balance between negative enthalpy change from bringing the charges closer and positive enthalpy change associated with removing the hydration shell.

The strength of the ion pair interactions will increase with temperature.

36
Q

Denaturation

A

Process where a structured biologically active molecule called the native form unfolds or becomes unstructured and biologically inactive

37
Q

Nucleotides

A

Subunits of nucleic acids
1. five C sugar (desoxyribose)
2. Nitrogen containing base
ring (pyrimidine single ring T U C or purine - > double ring A, G)

38
Q

Why is H-bonding between bases (in DNA) in water solution weaker than in organic solvents

A

Competition for H-bond formation with water

39
Q

RNA

A

linear polymer made of four different types of nucleotide subunits linked together by phosphodiester bonds with fcts in bio systems

40
Q

What interactions determine RNA structure

A

hydrogen bonding between bases, stacking interactions, hydrophobic interactions

Physics (6 decks)

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