Amino acids, Biology

Assignment Help:

 

  • An amino acid is amphiprotic (have both acid and base)

             o    Some are polar, non polar, acidic or basic

  • List of amino acids (red are non-polar, yellow are polar, green are acidic, blue are basic, starred are essential)

 

  •  An amino acid is amphiprotic (have both acid and base)

             o    Some are polar, non polar, acidic or basic

  •  List of amino acids (red are non-polar, yellow are polar, green are acidic, blue are basic, starred are essential)

 
                o    Glycine (gly)
                o    Alanine (ala)
                o    Valine (val)*
                o    Leucine (leu)*                                                                                    
                o    Isoleucine (ile)*
                o    Methionine(met)*
                o    Phenylalanine(phe)*
                o    Tryptophan (trp)*
                o    Proline (pro)

               o    Serine (ser)

 

                                                                1512_properties of Amino Acids.png1568_Amino Acids.png

 

               o    Threonine(thr)*
               o    Cysteine (cys)
               o    Tyrosine (tyr)

               o    Asparagines (asn)
               o    Glutamine (gln)
               o    Glutamic Acid (glu)
               o    Aspartic Acid (asp)

              o    Lysine (lys)*
              o    Arginine (arg)

              o    Histidine (his)

Properties of Amino Acids

Peptide Bond - bond between the acid group of one amino acid and the amino group of another
Dipeptide - 2 amino acids joined by a

peptide bond

  • Coded for by DNA and created by the ribosomes
  • Proteins are long, flexible and able to form different links with themselves or other molecules
  • Have an amino(A)-terminus and a Carboxyl(C)-terminus

Protein Structure

  • A Protein's function depends on its shape which depends on its amino acids

 

  • Primary Structure
    • Long chain of amino acids linked by covalent peptide bonds à in specific order
  • Secondary Structure
    • Intermolecular forces (mostly H-bonds) cause the chain to coil into an α-helix or fold into a β-pleated sheet
  • Tertiary Structure
    • Chaperone proteins help a growing polypeptide fold into its tertiary structure
    • Supercoiling due to polarity, the shape of the amino acids (e.g. proline causes a kink), other components (e.g. iron) and disulfide bridges.
  • Quaternary Structure
    • Various polypeptides join together with intermolecular forces to form a protein

Denaturing of Proteins

  • Change in è Heat, pH, temperature, ionic concentration etc.
    • Can cause changes in the 3-D structure of the protein

                        Change can be permanent if the 1° structure is broken

                        Change can be reversed if only the 3° structure is broken

  • Use of denaturing proteins à Food preservation

 

 

 


Related Discussions:- Amino acids

State in detail about the thylakoid membrane, State in detail about the thy...

State in detail about the thylakoid membrane The thylakoid membrane contains all the factors associated with the photosynthetic electron transport leading to the generation of

Find the highest homology among different species, Which level of a gene, s...

Which level of a gene, such as the ADH gene and its encoded product should have the highest homology among different species? Explain your answer. A. The genomic DNA sequences o

Defects of heart, DEFECT S OF HEART 1 .      Blue Baby syndrome (Cya...

DEFECT S OF HEART 1 .      Blue Baby syndrome (Cyanosis) - Due to persisting foramen ovalis in atrial septum even after birth, the impure blood from right auricles comes to

What are the clinical warning signs of implant failure, Clinical warning si...

Clinical warning signs of implant failure The clinical signs of implant failure are: 1) Connecting Screw loosening. 2) Connecting Screw failure. 3) Gingival bleeding a

Explain about the sucralose - artificial sweeteners, Explain about the Sucr...

Explain about the Sucralose - artificial sweeteners? Sucralose (1, 6-dichloro-1, 6-dideoxy-β-D-fructofuranosyl-4-chloro-4-deoxy-α-D- galactopyranoside) is the only non-nutritiv

What is the turnover number of the enzyme, Hydrolytic driving force. The hy...

Hydrolytic driving force. The hydrolysis of pyrophosphate to orthophosphate is important in driving forwards biosynthetic reactions such as the synthesis of DNA. THis hydrolytic re

Anther, parts and functions of the anther

parts and functions of the anther

Haccp control point, HACCP Control Point  HACCP Control Point :  Any...

HACCP Control Point  HACCP Control Point :  Any step at which biological, chemical or physical factors can be controlled.

Potential disadvantages - digitalis glycosides, Arrhythmias especially in p...

Arrhythmias especially in presence of hypokalemia, lack of mortality benefit. However, their efficacy in reducing the symptoms of heart failure has been established. Digoxin should

Plant, what is comretun

what is comretun

Write Your Message!

Captcha
Free Assignment Quote

Assured A++ Grade

Get guaranteed satisfaction & time on delivery in every assignment order you paid with us! We ensure premium quality solution document along with free turntin report!

All rights reserved! Copyrights ©2019-2020 ExpertsMind IT Educational Pvt Ltd