Chapter 9: Biomolecules Flashcards by Ashworks .

All the carbon compounds that we get from living tissues can be called _______________

Biomolecules

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Inorganic constituents present in living tissues are :-

Sodium (Na⁺
Potassium (K⁺
Calcium (Ca⁺⁺
Magmesium (Mg⁺⁺
Water (H₂O
Compounds (NaCl,CaCo³,PO₄^3-,SO₄^2-)

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Amino acids are organic compounds containing an amino group and an acidic group as substituents on the same carbon i.e the ____________

α-Carbon (Alpha carbon)

Hence, they are called α-amino acids

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There are Four substituent groups occupying the four valency position. these are Hydrogen , carboxyl group , amino group and a variable group designated as _________ in amino acids

R -group

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How may types of Amino acids which occur in Proteins

20 types

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The R group in proteinaceous amino acids could be a
Hydrogen in ________________
A methyl group in ___________
Hydroxy methyl in ___________

Glycine
Alanine
Serine

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Based on Number of amino and Carboxyl groups

there are acidic ______
Basic__________
and neutral _________ amino acids

Glutamic Acid
Lysine
Valine

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There are 3 Aromatic(Ring) amino acids are:- _____ , ________ and __________

Phenylalanine
Tyrosine
Tryptophan

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_________ is normally described as an ion containing two functional groups where the net formal charge of the molecule is zero.

Zwitterionic Form

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Lipids are generally water ________________

Insoluble

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A Fatty acid has a _________ group attached to an R group. The R group could be a methyl or ethyl or higher number of CH₂ groups (1 carbon to 19 carbons)

Carboxyl group

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Palmitic Acid has _____ carbons including the Carboxyl Carbon

CH₃-(CH₂)₁₄-COOH

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Arachidonic acid has ______ carbon atoms including the carboxyl Carbon

C₂₀H₃₂O₂

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Fatty acid could be __________(without double bond) and ___________(with one or more C=C double bonds)

Saturated

unsaturated

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Another simple lipid is ___________ whose chemical name is trihydroxy propane

Glycerol

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The Fatty acids are found esterified with _________ and then, they can be
Monoglycerides
diglycerides
Triglycerides

Glycerol

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Some Lipids have phosphorus and a Phosphorylated organic compound in them. These are _______________

Phospholipids

(they are found in Cell membrane)
ex:- Lecithin

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In Living organisms two types of Nitrogen Base are found :- _______ and __________

Purine
two carbon nitrogen ring fused together
Contain four nitrogen atoms in their structure
Adenine (A) and Guanine (G)

Pyrimidine
Contain a single carbon-nitrogen ring
Contain two nitrogen atoms in their structure
Cytosine (C), Thymine (T), and Uracil (U)

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When nitrogen base attached to a sugar they are called ____________, If phosphate group also found esterified to the sugar they are called __________

Nucleosides
Adnosine
guanosine
cytidine
thymidine
uridine

Nucleotides
Adenylic acid
guanylic acid
cytidylic acid
thymidylic acid
uridylic acid

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Nucleic acids like DNA and RNA consist of __________ only

Nucleotides

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__________ Metabolites are a type of metabolite that is closely engaged in the growth, development, and reproduction of an organism.

Primary

eg:- Carbohydrates, proteins, lipids, and vitamins

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_____________ Metabolites are compounds that are not directly engaged in normal growth and development but do have some ecological functions within the body.

Secondary

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compounds found in the acid soluble pool, the molecular weights ranging from ______ to _____ dalton (Da) approximately

18
800

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Chemical compounds which have molecular weights less than One Thousand dalton are usually referred to as ___________

Micromolecules or simply Biomolecules

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Chemical compounds which are found in the **acid insoluble fraction** are called ______________

**Macromolecules** or **Biomarcromolecules**

The **acid insoluble fraction**, has only four types of organic compounds i.e **protein, nucleic acids, Polysaccharides** and ___________ .these classes of compounds have molecular weights in the range of **Ten thousand** daltons and above **except** _____________

**Lipids** **Lipids** (Molecular weight do not exceed 800 **Da**(Dalton)

Average composition of cells where **Water** **Proteins** **Carbohydrates** **Lipids** **Nucleic acid** **Ions** **percentage** of the total cellular mass

**Water** 70-90% **Proteins** 10-15% **Carbohydrates** 3% **Lipids** 2% **Nucleic acid** 5-7% **Ions** 1%

**Proteins** are **Polypeptides**, they are linear chains of **Amino acids** linked by ______________

**Peptide Bonds**

Protein is a **Polymer** of ___________ , Protein is a **Heteropolymer** and not a **homopolymer**

**Amino acids** hint:- A **homopolymer** has only one type of monomer repeating **'n'** number of times.

There are _________ types of **amino acids**

**20**

**Dietary Proteins** are the source of _______________ amino acids

**Essential**

Some proteins which our body can make is known as ___________

**Non essential**

____________ is the most abundant protein in **Animal world** and ____________ is the most abundant protein in the whole of the **Biosphere**

**Collagen** **Ribulose bisphosphate Carboxylase-Oxygenase** (***RuBisCO***)

describe the function of following protein (**Don't** forget these are **Protein**):- **Collagen** **Trypsin** **Insulin** **Antibody** **Receptor** **GLUT-4**

**Collagen** - Intercellular ground substance **Trypsin** - Enzyme **Insulin** - Hormone **Antibody** - Fights infectious **Agent** **Receptor** - Sensory reception (smell, taste, hormone) **GLUT-4** - Enable **Glucose** transport into cells)

**Polysaccharides** (Carbohydrates) are long chains of ____________

**Sugar**

Cellulose is a polymeric polysaccharide consisting of only one type of **Monosaccharides**(simple sugar) i.e- _______________

**Glucose** (C₆H₁₂O₆)

**Cellulose** is a ___________ of **glucose** units linked together by **β-1,4-glycosidic bonds**, cellulose found in cell wall

**Homopolymer**

**Starch** is a variant of **glucose** present as a **store house of energy** in __________ tissue. **α-1,4-glycosidic bonds**

**Plant tissue**

**Animals** have another variant of **glucose** called _____________

**Glycogen**

**Inulin** is a polymer of ____________

**Fructose**

In a polysaccharide chain (Glycogen), the **right** end is called ___________ and the **left** end is called the _____________

**Reducing** end **Non- Reducing** end

**starch** forms __________ secondary structure, starch can hold _____ molecules in the helical portion. The ________ is **blue** in colour

**Helical** **I**_{2_{**Starch - I₂**}}

Cellulose does not contain complex helices and hence cannot hold ________

**I**₂

**Plant** Cell wall is made up of _______

**Cellulose**

**Paper** made from plant pulp and **Cotton fibre** is ____________

**Cellulose**

**Exoskeletons** of **arthropods**, have a complex **Polysaccharide** called ___________

**Chitin** These complex polysaccharides are mostly **Homopolymer**

For nucleic acids, the building block is a ____________

**Nucleotide**

A **nucleotide** has **three** chemically distinct components are Heterocyclic __________ base second is a ___________ sugar third is ________ acid

Heterocyclic nitrogenous base Monosaccharide Phosphoric acid or Phosphate

The **Heterocyclic** compounds in **Nucleic acids** are the ____________-

**Nitrogenous Bases** Adenine guanine cytosine thymine uracil

**Adenine** and **Guanine** are substituted __________ while the rest are substituted **Pyrimidines**

**Purines**

The **Sugar** found in polynucleotides is either __________(a monosaccharide **Pentose** or ____________

**Ribose** **2' deoxyribose**

A **Nucleic acid** containing **Deoxyribose** is called _______________ while that which contains **Ribose** is called _______________

**DNA** (Deoxyribonucleic Acid) **RNA** (Ribonucleic Acid)

The Sequence of **amino acids** i.e., the positional information in a protein -Which is the **first** amino acid, which is **second**, and so on - is called the ___________ structure

**Primary Structure**

A protein is imagined as a **line** (Primary structure) the left end represent by ________ amino acid and the right end represented by the ___________ amino acid

**First** (left) **Last** (Right)

The **first** amino acid is also called as _______ amino acid

**N-terminal amino acid**

The last amino acid is called the _______

**C-terminal amino acid**

In **Protein**, only ________ handed helices are observed

**Right**

Regions of the protein thread are folded into other forms in what is called the ____________structure

**Secondary**

The long protein chain is also folded upon itself like a hollow woolen ball, gives rise to the _____________ structure, This gives us a **3- dimensional* view of protein

**Tertiary structure**

Some proteins are an assembly of more than on **Polypeptide or subunits** , the manner in which these individual folded polypeptides or subunits are arranged with respect to each other is called __________ structure

**Quaternary Structure**

Adult human haemoglobin consists of 4 subunits, two of these are identical to each other . two subunits of α-type and two subunit of ß-type together constitute the human haemoglobin (Hb) is example of _________structure.

**Quaternary Structure**

Almost all **enzymes** are ___________

**Protein**

There are some **nucleic acid** that behave like enzymes, these are called ____________

**Ribozymes**

The backbone of the **protein**(enzyme) chain folds upon itself, the chain criss-crosses itself and hence many crevices or **pockets** are made. One such pocket is the ___________

**Active site**

Enzymes, through their **Active site** catalyze reactions at __________rate

**High**

Enzymes get damaged at **high temperatures** say above __________ ^oC

**40^o C**

Enzymes isolated from organisms who normally live under extremely high temperatures (e.g hot vents and Sulphur springs) are stable and retain their catalytic power even at high Temperature upto __________ **^oC**

**80^o - 90^o C**

Chemical compound change in shape without breaking of Bonds are called ___________ when bonds are broken and the new bonds are formed during transformation, this is called ___________

**Physical process or physical change** **Chemical Reactions**

Rate of **physical or chemical process** refers to the amount of ________per unit time

**Product formed** rate=P/T rate can also be called **velocity** if the direction is specified

**Rate of chemical and physical process** are influenced by temperature , A general rule of thumb is that rate **doubles** or **decreases by half** for every ______^oC change in either direction

10^o C

In absence of any enzyme reaction is very slow, about **200 molecules** of **H₂CO₃ Carbonic Acid** being formed in an **hour** (in cell using carbon dioxide + water) by using enzyme present within the cytoplasm called ___________ the reaction speeds dramatically with about 600000 molecules formed every **Second** The enzyme has accelerated the reaction rate by about **10 million** times

**Carbonic Anhydrase**

A **multistep** chemical reaction, when each of the steps is catalysed by the same enzyme complex or different enzymes, is called ___________

**Metabolic Pathway** Glucose -> 2 Pyruvic acid (C₃H₄O₃)

In our skeletal muscle, under **anaerobic** condition _________ is formed. under normal **Aerobic condition** _____________ is formed. In yeast, during fermentation, the **same pathway** leads to the production of __________

**Lactic acid** **Pyruvic Acid** **Ethanol** (Alcohol)

The chemical which is converted into a product is called _______

**Substrate**

**Enzymes i.e. protein** with **three dimensional** structures including an **'active site'** , convert a **Substrate (S)** in a ___________

**Product**

The substrate **'S'** has to bind the enzyme at its _________within a given cleft or pocket

**Active site**

The structure of substrate gets transformed into the structure of Product. The pathway of this transformation must go through the so-called ___________

**Transition state structure**

There could be many more **'Altered structural states'** between the stable substrate and the __________________

**Product**

The energy that is needed to get a reaction **started** is called ____________

**Activation energy**

whether it is an exothermic or spontaneous reaction or an endothermic or energy requiring reaction. the Substrate has to go through a much **higher energy state** or _______________ . The difference in average energy content of Substrate from that of this transition state is called _____________

**Transition state** **Activation energy**

If Product is at a lower level than Substrate the reaction is an ___________

**Exothermic Reaction**

If product is at higher level than Substrate the reaction is an _____________

**endothermic reaction**

E + S ES ------------>EP------------E + P what is E + S , ES , EP and E + P in enzyme action

**E + S**-- (Substrate binds to enzyme at active site) **ES** --(Enzyme-substrate complex) **EP** --(Enzyme-product complex) **E + P**--(enzyme releases the product)

Each Enzyme shows its highest activity at a particular **Temperature** and **pH** called the ___________ and ____________

**Optimum Temperature** **Optimum pH**

Below and Above **optimum value** enzyme Activity ___________

**Declines**(decrease)

In _________ temperature the enzyme gets temporarily in **Inactive State**

**Low** (Preserves there structure)

**High Temperature destroys** enzymatic activity because ___________ are denatured by heat

**Proteins**

With the increase in **substrate concentration**, the velocity of the enzymatic reaction___________ at first reaches max velocity (V_max), then no further rise because the enzyme molecules are fewer than the substrate molecules

**Rises**

The activity of an enzyme is also sensitive to the presence of specific chemicals that bind to the enzyme, When the binding of the chemical **shuts off** enzyme activity , the process is called ____________ and the **chemical** is called __________

**Inhibition** **Inhibitor**

When the **inhibitor** closely resembles the substrate in its **molecular structure** and inhibits the activity of the enzyme , It is known as ______________

**Competitive inhibitor**

Inhibition of **Succinic dehydrogenase**( Enzyme) by ___________ which closely resembles the **Substrate** ____________ in structure. Such competitive inhibitors are often used in the **Control** of **Bacterial pathogens**

**Malonate** **Succinate**

Enzymes are divided into ____________ classes each with 4-13 subclasses and named accordingly,

**6 - classes**

What are the function of these enzymes **Oxidoreductases/dehydrogenases Transferases hydrolases lyases Isomerases Ligases**

**Oxidoreductases/dehydrogenases**-Enzymes which catalyse oxidoreduction between two substrates **Transferases**- Enzymes catalysing a **transfer** of group (other than hydrogen) between two substrate **hydrolases**- Enzyme catalysing hydrolysis of **ester**,ether, peptide, glycosidic, P-N bonds **lyases**- **Removal** of groups from substrates by mechanisms other than hydrolysis leaving **double bonds** **Isomerases**- enzymes catalyzing **inter-conversion** of optical, geometrical or position isomers. **Ligases**-Enzymes catalysing the **linking** together of 2 compounds which catalyse joining of C-O,C-S,C-N

Enzymes are composed of one or several polypeptide chains, there are a number of cases in which **non-Protein** constituents called ___________ are bound to the enzyme to make the enzyme catalytically active. In these enzymes the **Protein portion** of the enzymes is called the ____________

**Co-factors** **Apoenzymes**

Three kinds of **Co-factors** are identified: **Prosthetic groups**, Co-enzymes and _____________

**Metal ions**

**Prosthetic groups** are organic compounds and are distinguished from other cofactors in that they are **tightly bound** to the ____________

**Apoenzyme** eg- peroxidase and catalase

_________________ are also organic compounds but their association with the **apoenzyme** is only **transient**

**Co - Enzymes** The essential chemical components of many co-enzymes are **Vitamins** eg:- coenzyme nicotinamide adnine dinucleotide (NAD) and NADP contain the vitamin **Niacin**

A number of enzymes require metal ions for their activity which form _______________ bonds with side chains at the active site and at the same time form one or more __________ bonds with the substrate

**coordination** Zinc is a cofactor for the Proteolytic Enzyme **Carboxypeptidase**

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Chapter 9: Biomolecules Flashcards

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