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

Energy loss - energy flow, Energy Loss - Energy Flow Let us now take t...

Energy Loss - Energy Flow Let us now take the second point that is the loss of some energy at each trophic level. You might recall that the second law of thermodynamics states

Describe the advantages of sulphur, Describe the advantages of sulphur ...

Describe the advantages of sulphur Sulphur also increases the oil content of crops such as flax and soyabeans. Disulphide linkages ( -S-S-) have recently been associated with

Determine the modification of native starch, Determine the Modification of ...

Determine the Modification of native starch Modification of native starch can be either physical or chemical. Chemical modification includes reaction of starch with  acid or al

Determine the interphase of mitosis, Is the interphase of meiosis differen...

Is the interphase of meiosis different from the interphase of mitosis? The interphase that precedes meiosis is same to the interphase that precedes mitosis. In them the major e

Assessment of acute rheumatic fever, Assessment   While assessing the p...

Assessment   While assessing the patient with rheumatic fever, a detailed history including, problematic environmental factors or recent exposure to streptococcal infection is

Which technique would use to see if a particular protein, Which technique w...

Which technique would you use to A) see if a particular protein bound to a piece of DNA B) Detect exactly where on a piece of DNA a protein bound.

Eye drops, Eye Drops Medication is instilled in the form of drops or ...

Eye Drops Medication is instilled in the form of drops or ointment.   Purpose To dilate pupil e.g. Atropine 1 per cent, drosyn 5 per cent or 10 per cent  To c

Pathogenesis, The interactions between the human host and selected microorg...

The interactions between the human host and selected microorganisms that culminate in IE involve the vascular endothelium, hemostatic mechanisms, the host immune system, gross anat

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