Protein Types and Functions

<p>Globulin (A)</p> Signup and view all the answers

<p>Energy storage (A)</p> Signup and view all the answers

<p>Simple proteins (D)</p> Signup and view all the answers

<p>N-terminal and C-terminal (D)</p> Signup and view all the answers

<p>Structural proteins (C)</p> Signup and view all the answers

<p>Presence of non-protein parts (B)</p> Signup and view all the answers

<p>Antibody (C)</p> Signup and view all the answers

<p>Iron transport (B)</p> Signup and view all the answers

<p>A storage form of iron (A)</p> Signup and view all the answers

<p>Hemoproteins (A)</p> Signup and view all the answers

<p>Primary derivatives result from denaturation, while secondary arise from hydrolysis. (D)</p> Signup and view all the answers

<p>A primary protein derivative (B)</p> Signup and view all the answers

<p>Proteins associated with nucleic acids (B)</p> Signup and view all the answers

<p>Peptide bonds are cleaved. (D)</p> Signup and view all the answers

<p>Peptone (C)</p> Signup and view all the answers

<p>Hydrogen carrier (D)</p> Signup and view all the answers

<p>Denaturation occurs without peptide bond breakage (C)</p> Signup and view all the answers

<p>Deficient in essential amino acids such as tryptophan (A)</p> Signup and view all the answers

<p>Coagulation changes protein structure from liquid to solid (B)</p> Signup and view all the answers

<p>Gelatin (D)</p> Signup and view all the answers

<p>Carbohydrates (C)</p> Signup and view all the answers

<p>Ceruloplasmin (A)</p> Signup and view all the answers

<p>Transporting lipids in the blood (A)</p> Signup and view all the answers

<p>Phosphoprotein (C)</p> Signup and view all the answers

<p>It is solubilized in water (A)</p> Signup and view all the answers

<p>Complete essential amino acid profile (B)</p> Signup and view all the answers

<p>Immune response (C)</p> Signup and view all the answers

Organic complex nitrogenous compounds formed from C, H, O, N (sometimes S), combining amino acids into polypeptide chains.

Polypeptide chains of amino acids linked by peptide bonds (-CO-NH-), with a C-terminal end and an N-terminal end.

The link between amino acids in proteins, formed from a carbonyl group and an amine group.

A protein that, when chemically broken down (hydrolyzed), only consists of amino acids.

Simple proteins, conjugated proteins, and derived proteins categorize them according to their components.

Proteins that contain non-protein components (prosthetic groups) besides amino acids.

Proteins produced from the breakdown of simple or conjugated proteins.

Biological catalysts that speed up chemical reactions in living organisms.

Chemical messengers that regulate various bodily functions.

Proteins play crucial roles in various biological functions, including structural support, enzymatic catalysis, and regulation.

Change in protein structure from liquid to solid or thicker liquid.

Obtained from collagen by boiling.

Easily digested.

Low biological value; Deficient in some amino acids (e.g., tryptophan).

Contain all essential amino acids (e.g., casein, albumin, globulin).

Lack one or more essential amino acids (e.g., gelatin, gliadin, vegetable proteins).

Hormones, antibodies, blood group antigens, receptors, and enzymes.

Lipid transport in blood.

Caseinogen (milk protein).

A protein responsible for transporting iron (Fe+2) in the blood.

A protein that stores iron (Fe+3) in the body.

A hormone that regulates blood glucose levels by allowing cells to take up glucose.

A protein that contains a colored pigment.

A chromoprotein that transports oxygen in the blood.

A chromoprotein that stores oxygen in muscle tissue.

A chromoprotein containing flavin pigments, involved in electron transfer.

A protein complexed with nucleic acids (DNA or RNA).

Products of protein denaturation, where the peptide bonds remain intact.

Products of protein hydrolysis, where the peptide bonds are broken, resulting in smaller peptides or amino acids.