biochemistry test

Entropy

Mess. change of S

Enthalpy

Energy. Chape of H

Free Energy

ability to do work

1st law of thermodynamics

energy cannot be created or broken

2nd law of thermodynamics

Entropy will always reach max values

Where does Homeostasis get energy from

NADH, FADH, ATP

Coupling

Positive and negative situations combine to make the most stable.

stereoisomers

same formula but different physicality

geometric isomers

different shape, similar formula,

enantiomer

mirror images but not the same

disantiometer

different everything

PI

isoelectricic point at which aminos PH is 0

Zwiterrion

Amino Acid with the PH of 0

SHam, OHver, NHine, COOcH, CHOrro, Cuz He OHver, CHarged

SH>OH>NH2>COOH>CHO>CH2OH>ch3

protein percentage in body

40% in skeletal muscles and 25% in organs

function of protein

catalyst, motion, structure, transportation

proteins in membranes

hydrophobic

fibrous protein

atypical

native fold is most stable with

alot of unsta

when does is protein shaped

ribosome synthesis

anabolism increases when

eating

protein synthesis increases when

after exercise

configuration

change with breaking bonds

conformation

cha

prosthetic groups

important groups that are not amino acids

post translational

chemical change after sy

Native Fold

3D configuration of proteins

**Hydrophobic interactions drive what**

 **protein folding**

Describe the bonds for a helix

parallel

Is a helix hydrophobic or hydrophilic

Both

**β sheet**: H bonds are both

parallel and antiparallel

What hydrogen bonds are stronger parallel or anti parallel

Anti-parallel since they are more linear

most common regular secondary structures are

alpha-helix, beta sheets, and beta turns.

what exactly is the beta turn?

180 degree turn over 4 amino acids \n (carbonyl of AA1 is bonded to amide of AA4)

glycine and proline are common for a beta turn- why?

glycine and proline are common because glycine is flexible so it can handle the turn, proline gives it a kink so it can actually make the turn

**Three main types** of fibrous protein:

**α-Keratin, β-Keratin, Collagen**

**Cofactor**

**Inorganic ions that attach to protein portion of enzyme**

Coenzyme

(vitamin) complex organic or metalloorganic molecule that act as carriers of functional groups

**Prosthetic group**

A coenzyme or metal ion tightly or **covalently bound** to the enzyme (heme)

**Holoenzyme =**

enzyme together with its bound coenzyme/metal ion (glutathione reductase with Se-)

__**Apoenzyme/apoprotein**__

the protein part of an enzyme (lipoproteins

Vitamin C (ascorbic acid) is a cofactor

for proline hydroxylation; the base of collagen

globular protein composition

**polar residues face the outside** and **hydrophobic residues face the interior**

Proteins can be denatured by:

Heat or cold, pH extremes, Organic solvents

nonprotein components essential to enzyme activity.

**Coenzymes and cofactors**