All proteins contain the following elements EXCEPT

What element separate proteins from lipids and carbohydrates?

Essential constituent of certain specialized protein

protein

All amino acids are alpha-amino acids

Glycine (Gly, G) is

Alanine (Ala, A) is a

Valine (Val, V) is a

Leucine (Leu, L) is a

Isoleucine (Ile, I) is a

Proline (Pro, P) is a

Phenylalanine (Phe, F) is a

Methionine (Met, M) is a

Trytophan (Trp, W) is a

Serine (Ser, S) is a

Cysteine (Cys, C) is a

Threonine (Thr, T) is a

Asparagine (Asn, N) is a

Glutamine (Gln, Q) is a

Tyrosine (Tyr, Y) is a

Aspartic Acid (Asp, D) is a

Glutamine acid (Glu, E) is a

Histidine (His, H) is a

Lysine (Lys, K) is a

Arginine (Arg, R) is a

These set of amino acids are found inside the protein and interact with lipids

These set of amino acids are found outside of protein and function inside the membrane. Also known as associated proteins

also known as polar negative amino acid

also known as polar positive amino acid

This amino acid is needed for protein synthesis but the human body is unable to create enough amount for itself.

Essential amino acid that is needed for children's growth but not for adult

I have all the essential amino acids but I may not have all the non essential amino acid. Who am I?

I don't have adequate amount of essential amino acids

I am the essential amino acid that is missing in an incomplete amino acid

I am made up of two or more incomplete dietary protein

This kind of bond is formed by a biochemical reaction that extracts water molecule as it joins the amino group of one amino acid to the carboxylic group of the neighboring amino acid.

Also known as amide bond

Peptide bond is a

Depends directly on the linear amino acid sequence of the protein

The linear amino acid sequence is the

How many sets of amino acids does the protein have

The largest group of amino acid has ______ side chains

Charged amino acids can form ______ bonds

Polar amino acid side chains can form ______ bonds

Hydrophobic side chains can form ______ bonds

Charged amino acid side chains can form ______ bonds

I am the amino acid that is capable of forming a covalent bond

has 2 or more amino acids

has 3 or more amino acids

has 10 or 20 more amino acid residues present in a chain

Step by step peptide formation:

I. Two amino acids are brought together.

II. The peptide bond is left between the two amino acids and the chain continue

III. A water molecule is eliminated

Peptide nomenclature (IUPAC)

The amino acid sequence begins at the C-terminal amino acid residue

Peptide nomenclature (IUPAC)

The -yl suffix replaces the -ine or -ic acid ending of the amino acid name

Peptide nomenclature (IUPAC)

The C-terminal amino acid residue keeps its full amino acid name

Uterus contracting hormone (also stimulates lactation)

found in most living cells as antioxidant and promote tissue growth

inhibits growth hormone release

(used to treat ulcer)

Honey bee venom

(used to treat rheumatism *sakit sa joints)

Enhances reabsorption of free water.

Plays an important role in BP control.

Hypothalamic neurohormone.

Governs the release of TSH.

Hypotensive vasodilator.

Acts on smooth muscle.

Hypotensive vasodilator.

Acts on smooth muscle.

Hyperglycemic Factor.

Used as anti-diabetic.

Pain killers.

Neuromodulator in the brain and spinal cord.

Angiotensin II

Potent vasoconstrictor.

Structurally similar to snake venom.

Pancreatic hormone.

Used in treatment of diabetes

protein that enable female mammals to produce milk

It is the structure of protein that drives the folding and intramolecular bonding of the linear amino acid chain.

These determines the protein's 3-D shape.

Held by covalent peptide bonds

Made up of stable folding patterns or the alpha helices and beta sheets

This structure is made up of polypeptide or formations and folds in a single linear chain of amino acid.

Refers to the macromolecules with multiple polypeptide chains or subunits.

alpha helices and beta sheets are products of what kind of bond?

in the Quaternary protein structure:

1.The two or more polypeptide chain is structurally identical with each other.

2.The two or more polypeptide chain is totally unrelated with each other.

Protein folding involves ______ pathways

What structure is formed as the peptide folds

The formation of secondary structure is driven by hydrophobic effect (when hydrophobic groups come together as water is released)

Amino acids with positively and negatively charged side chains__________each other

Hydrogen bonding involves

Hydrophobic interaction involves

Disulfide bonds involves

In the _______, the peptide achieves its fully folded, native form characterized by ______ energy state.

These proteins or segments lack a stable tertiary structure.

Protein denaturation results in the unfolding and disorganization of protein's _____ structure and _____structure which are not accompanied by hydrolysis of peptide bonds.

Denaturing agents

Denaturation is irreversible

Denatured proteins are often insoluble

The formation needed for proper protein folding is found in

Many proteins are facilitated by_____to resume their native conformation

I am helper protein, but you can also call me

Chaperones can

Proteins are classified based on the

Monomeric protein only have one peptide chain.

One example is

Multimeric protein have more than one peptide chain.

What do you call these peptide chains?

Chemical composition of protein that include substances formed from simple conjugated protein

Chemical composition of protein that has one or more non-amino acid entities

Chemical composition of protein that only have amino acid residues

Albumin has a chemical composition of a

Conjugated protein has one or more non-amino acid entities.

What do you call these groups of non-amino acid entities?

A protein derivative which have undergone slight intramolecular rearrangement and is synonymous with denatured protein

It is a secondary protein derivative that is precipitated by conc.HNO3 and by half saturation with (NH4)2SO4 or ZnSO4 but not coagulated by heat.

It is a secondary protein derivative that is precipitated only by complete saturation with (NH4)2SO4 but nit with picric acid and HNO3

It is a secondary protein derivative that is NOT precipitated by saturation with (NH4)2SO4 but saturated by a certain ALKALOIDAL reagent.

(posphotingstic and tannic acid)

Fibrous protein has

Globular protein has

There are 2 kinds of protein based on its shape, fibrous and globular.

Which of the following is the characteristic of a fibrous protein?

This Protein Energy Malnutrition (PEM) occurs when protein reduction is greater than total calorie reduction.

This Protein Energy Malnutrition (PEM) occurs when total calorie reduction is greater than the protein reduction.

This Protein Energy Malnutrition (PEM) occurs when the child's diet consist predominantly of carbohydrates.

This Protein Energy Malnutrition (PEM) occurs when breastmilk is supplemented with cereals that usually lacks in protein and calories.

This Protein Energy Malnutrition (PEM) do not show edema or changes in plasma proteins.

GWAPO SI ALFRED