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Introduction to Thermodynamics and Biochemistry: Gibbs Free Energy, Proteins, and Buffers, Quizzes of Social Anthropology

Towson University (TU)Social Anthropology

Definitions and explanations of key concepts related to gibbs free energy, including delta g, delta h, delta s, standard gibbs energy, and the role of gibbs free energy in making unfavorable reactions favorable. The document also covers the hydrolysis of atp, amphipathic molecules, acids and bases, buffer effect, and the structure and function of amino acids and proteins. Terms related to protein structure, including primary, secondary, tertiary, and quaternary structures, are also discussed.

Typology: Quizzes

2013/2014

Uploaded on 09/23/2014

rachelazamora
rachelazamora 🇺🇸

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TERM 1
Gibbs Free
Energy
DEFINITION 1
delta G= deltaH - TdeltaS
TERM 2
G*
DEFINITION 2
gibbs free energy at STANDARD CONDITIONS
TERM 3
delta H
DEFINITION 3
Enthalpythe energy stored in a bond = + positivethe energy
released = - negativeheat released
TERM 4
Delta S
DEFINITION 4
Enthalpymeasure of disorganizationfavorable = +positive =
more disordernegative - = less disorder
TERM 5
Standard Gibbs Energy
Equation
DEFINITION 5
delta G* = - RT ln Keq
pf3
pf4
pf5
pf8
pf9
pfa
pfd
pfe
pff

Partial preview of the text

Download Introduction to Thermodynamics and Biochemistry: Gibbs Free Energy, Proteins, and Buffers and more Quizzes Social Anthropology in PDF only on Docsity!

Gibbs Free

Energy

delta G= deltaH - TdeltaS

TERM 2

G*

DEFINITION 2

gibbs free energy at STANDARD CONDITIONS

TERM 3

delta H

DEFINITION 3

Enthalpythe energy stored in a bond = + positivethe energy

released = - negativeheat released

TERM 4

Delta S

DEFINITION 4

Enthalpymeasure of disorganizationfavorable = +positive =

more disordernegative - = less disorder

TERM 5

Standard Gibbs Energy

Equation

DEFINITION 5

delta G* = - RT ln Keq

R=

8.314 J/mol * K

TERM 7

Standard Condition

DEFINITION 7

1 atm25*C = 298 K1 Molar Product & Reactants

TERM 8

Gibbs when not at standard conditions

equation

DEFINITION 8

delta G = G* + RT ln QQ= [Products]/ [Reactants] at moment

not at equilibrium

TERM 9

How to make unfavorable reactions

favorable?

DEFINITION 9

-change concentrations-couple unfavorable with extremely

favorable reactions to make a relatively favorable reaction

TERM 10

ATP hydrolysis

DEFINITION 10

ATP --> ADP + Pioccurs when you add H20FAVORABLE

What is the main buffer in blood

BicarbonateH2Co3 --->.<-- h20 + CO

TERM 17

Buffering capacity on graph?

DEFINITION 17

look at where the pkas are and then +/- 1 pH is the buffering

capacity

TERM 18

what is the pH in blood?

DEFINITION 18

TERM 19

less than 7.

pH

DEFINITION 19

acidosis

TERM 20

more than

DEFINITION 20

alkalosis

Zwitterion

neutral molecule with positive and negative charge to make

neutral compound

TERM 22

All Amino Acids are ________

DEFINITION 22

L - stereoisomers

TERM 23

Structure of AA

DEFINITION 23

Amino groupCarboxylic AcidHydrogen = into the boardSide

Chain R = out of the board

TERM 24

pKa of amino group

DEFINITION 24

TERM 25

pKa of carboxylic acid

DEFINITION 25

Base / Buffer

LysineArginineHistidine

TERM 32

Peptide Bond

DEFINITION 32

covalent bond when carboxyl group binds with an amino

groupthis forms resonance

TERM 33

Sequence of Proteins

DEFINITION 33

only points of flexibility are at alpha carbons

TERM 34

Primary Structure

DEFINITION 34

sequence of amino acids

TERM 35

Motifs

DEFINITION 35

sequence of amino acids for a common purposespecific

conserved sequence

Secondary Structure caused by?

alpha helixbeta sheetloop*all caused by strain made by

peptide bonds

TERM 37

alpha helix structure

DEFINITION 37

N Terminus at bottomC Terminus at topbases / amino H's

point downhydrogen bonds are verticalcarbonyl =0 points up

TERM 38

What is in the N-Cap of alpha helix?

DEFINITION 38

Proline

TERM 39

What is in the C Cap of alpha helix?

DEFINITION 39

Proline

TERM 40

Beta Sheet - Parallel sheets describe

hydrogen bonds

DEFINITION 40

Hydrogen bonds are oblique angles

Super Secondary Structure (2)

2) Helix-turn- Helix2 alphas joined by turnmajor way proteins

"READ" DNAone helix fits into the major groove of DNA, the

other helix helps position first

TERM 47

Primary structure is ____

DEFINITION 47

linear

TERM 48

Secondary structure have proteins interact

via ____

DEFINITION 48

backbone

TERM 49

Tertiary Structure

DEFINITION 49

AlphaBetaAlpha-Beta

TERM 50

Describe tertiary structures

DEFINITION 50

determines interactionsinternal AA are hydrophobicexternal

AA are hydrophilicloops tend to be hydrophilic

Tertiary structure is sealed by...

SALT BRIDGESDISULFIDE BONDSMETAL IONS

TERM 52

can tertiary structures be undone?

DEFINITION 52

YESbecause not covalent bondsmay be undone & denatured

TERM 53

How to denature?

DEFINITION 53

temperaturepHovercoming "hydrophobic effect" via

detergents, via chaotropic agents

TERM 54

Chaotropic Agents

DEFINITION 54

disrupt H bonding between H20 moleculesex: Urea

TERM 55

Quaternary Structures

DEFINITION 55

multiple proteins coming togetherEach step exists in

equilibriumsome proteins function at semi-folded state

When a protein binds to a Ligand

-conformational change-regulate protein function-no

reaction-catalyze a reaction

TERM 62

Van Der Walls

DEFINITION 62

non-polar electron clouds that snuggle

TERM 63

P + L -->

DEFINITION 63

[P:L]

TERM 64

Equilibria or Association equation

DEFINITION 64

KA= [P:L] / {[P][L]

TERM 65

Proteins interact with Ligands to form ______

DEFINITION 65

Equilibrium

P:L yields?

P + L

TERM 67

Kd

DEFINITION 67

Dissociation CoefficientMolarityStrong Affinity = nano molar

10^-9Weak Affinity = millimolar 10^-

TERM 68

Affinity =

DEFINITION 68

A preference of a protein for a ligand is it's affinity for that

ligand

TERM 69

Kd equation

DEFINITION 69

Kd = 1 / Ka

TERM 70

Dissociation first order

DEFINITION 70

k [P:L]=Kd