Biochemistry Metabolism Of Proteins 1

Front 1

What are amino acids?

Back 1

Amino acids are biologically important organic compounds composed of (-NH2 and (-COOH) functional groups, along with side chains specific to each amino acid. The key elements are carbon, hydrogen, oxygen and nitrogen

Front 2

Amino acids join via?

Back 2

Peptide bonds

Front 3

What are the classification of amino acids?

Back 3

Non-polar amino acidsPolar, uncharged amino acidsAcidic amino acidsBasic amino acids

Front 4

What are the non Polar amino acids

Back 4

Hint 4

VALP

Front 5

What are the polar, uncharged amino acids

Back 5

Hint 5

SAGG

Front 6

What are the Acidic amino acids

Back 6

Hint 6

TAGMIP

Front 7

What are the basic amino acids

Back 7

Hint 7

LACHTT

Front 8

List the uncommon amino acids

Back 8

- Hydroxylysine, hydroxyproline - collagen

- Carboxyglutamate - blood clotting proteins

- Pyroglutamate - bacteriorhodopsin

- Phosphorylated amino acids - signaling device

Front 9

Describe the reactions of amino acids

Back 9

-Carboxyl groups form amides & esters

-Amino groups form Schiff bases and amides

*Side chains show unique reactivities

-Cys residues can form disulfides and can be easily alkylated

-Few reactions are specific to a single kind of side chain

Front 10

Describe the stereochemistry of amino acids

Back 10

-All but glycine are chiral

-L-amino acids are predominate in nature

-D, L- nomenclature is based on glyceraldehyde

Front 11

Describe the spectroscopic properties of amino acids

Back 11

- All amino acids absorb in infrared region

- Only Phe Tyr and Try absorb UV

- Absorbance at 280 nm is a good diagnostic device for amino acids

- NMR spectra are characteristic of each residue in a protein, and high resolution NMR measurements can be used to elucidate 3-D structures of proteins

Front 12

Name two methods of separating amino acids

Back 12

- Ion exchange chromatography

- High performance liquid chromatography

Front 13

List the essential proteins according to their properties

Back 13

branched chain: Val, Leu, Ilearomatic: Phe (→ Tyr), Trpbasic: His, Arg, Lys sulfur-containing: Met (→ Cys)other: Thr

Hint 13

PVT TIM HALL

Front 14

List the non essential amino acids

Back 14

Gly, Ala, Pro, Ser, Tyr, Asn, Gln, Asp, Glu, Cys

Front 15

Proteins provide?

Back 15

- Amino acids for protein synthesis

- Nitrogen atoms for nitrogen containing compounds

- Energy when carbohydrate and lipid resources are not available

Front 16

Peptide bond?

Back 16

-Amide bond so stable

- Amino group condenses with acid group

-

Front 17

Describe the classification of amino acids

Back 17

- Simple: hydrolyze to amino acids only

- Conjugated : bonded to non protein group such as sugar, nucleic acid, or lipid

- Fibrous: long, stringy filaments, insoluble in water, function as structure

- Globular: folded into spherical shape, function as enzymes, hormones, or transport proteins

Front 18

Describe primary structure

Back 18

Sequence of amino acids

Front 19

Describe secondary structure

Back 19

Interactions that occur between the c=o and N-H groups on amino acids

Much of the protein core comprises  helices and  sheets, folded into a three-dimensional configuration: - regular patterns of H bonds are formed between neighboring amino acids- the amino acids have similar angles

- the formation of these structures neutralizes the polar groups on each amino acid- the secondary structures are tightly packed in a hydrophobic environment- Each R side group has a limited volume to occupy and a limited number of interactions with other R side groups

Front 20

Describe Transamination

Back 20

Mechanism for conversion of non-essential amino acids into keto acidsEnzymes are aminotransferases or transaminasesTransfer of amino group from one amino acid into keto acid

Front 21

Describe tertiary structure

Back 21

Organization in three dimensions of all the atoms in the polypeptide

A. Fibrous proteins

B. Globular proteins

Front 22

Describe quaternary structure

Back 22

Confirmation assumed by a multimedia protein

The individual polypeptide chains that make up a multimeric protein are often referred to as protein subunits.

Subunits are joined by ionic, H and hydrophobic interactions

Front 23

Describe alpha helix

Back 23

Each carbonyl oxygen can form hydrogen bond with an N-H hydrogen on the next turn of the coil.

Front 24

Describe beta pleated sheet

Back 24

Each carbonyl oxygen hydrogen bonds with an N-H hydrogen on an adjacent peptide chain.

Front 25

List other secondary elements

Back 25

-random coil

-loop

-310 helix

-B- hairpin

-Paper clip

Front 26

Describe super-secondary structure

Back 26

There are some structural motifs in some proteins

These structures can give important hints about protein function

Eg, transmembrane domains

Coiled coils

Helix-turn-helix

Signal peptides

Front 27

Describe two structural classification of proteins

Back 27

Type 1:

Mainly alpha

Mainly beta

Alpha/beta

Few secondary structure

Type 2:

Class alpha

Class beta

Class a/B

class A/b

Membrane structure

Multidomain

Front 28

Describe denaturation

Back 28

- Disruption of the normal structure of a protein, such that it loses biological activity.

- Usually caused by heat or changes in pH

- Usually irreversible

Front 29

List the steps for protein metabolism

Back 29

1) Transamination

2) Oxidative Deamination

Front 30

Describe Transamination

Back 30

Mechanism for conversion of non-essential amino acids into keto acidsEnzymes are aminotransferases or transaminasesTransfer of amino group from one amino acid into keto acid

Front 31

Describe Oxidative deamination

Back 31

Front 32

Summarize the urea cycle

Back 32