why is CF mucus so sticky

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  • Created by: Leigh. x
  • Created on: 11-10-12 10:52

General Structure

  • There are 20 different types  of amino acids

  • The H-N-H part is known as the amino group
  • The COOH part is known as the carboxyl group
  • The R group is a variable group and determines the property of an individual amino acid.
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Dipeptide

- Two amino acids bonded together.

  • They are bonded together by a Condensation reaction. The reaction occurs between the carboxyl group of one amino acid and the amino group of another amino acid. This is seen below. The bond is called the peptide bond.

(http://t2.gstatic.com/images?q=tbn:ANd9GcSscptuU1Xu3Q3Gn2vBQK6Dsiu18UiqzkCuDIQBnCnUWa84yqQs)

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Peptide bond

The peptide bond holds a dipeptide together. When the bond is formed water H20 is lost.

Features of the bond

  • Its stable/ strong
  • Hydrolysis ( breaking apart using water) is the only way to break them.
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Primary Structure

Primary structure is the order or sequence of amino acids in a long polypeptide chain

The primary structure is VERY important, if it is wrong the whole structre and unique shape of a protein changes

(http://w3.hwdsb.on.ca/hillpark/Departments/Science/Watts/SBI3U/Class_Summary/Protein_-_Primary_Structure.jpg)

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Secondary Strucure

  • Hydrogen bond - can be made between a lot odf amino acids. its quite a weak bond however there are lots of them making the structure strong.

Arrangements :

Alpha Helix:- A very common strucutre, its very stable ( due to the presence of a lot of hydrogen bonds

(http://t1.gstatic.com/images?q=tbn:ANd9GcTjYw2otzHC2QU3tr4bdRqGyvbu2V7lSFCBSKHHoC_mJbi4WbXz3g)(http://t2.gstatic.com/images?q=tbn:ANd9GcRYhiOKVMuZwi7D5elv9a6FKYUhZoKeXAu4Ab8eVnpC3ek8JLRDWQ)

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Secondary Structure

Beta pleated sheet ( a stable structure)

(http://faculty.ccbcmd.edu/courses/bio141/lecguide/unit3/viruses/images/betasheet.jpg)

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Tertiary Structure

A tertiary structure is a single continuos peptide chaind in which several alpha helices tubes are arranged and parts of irregualr folding which allows it to turn and twist.

(http://t3.gstatic.com/images?q=tbn:ANd9GcQkkJRj4zOzEhDoskSY1kezuGK0xtOKBZB3dfzrF_-svWbuJpfj)

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Bonds involved in tertiary structures

  • The strucutre is very weak - if you heat up the structure, bonds break and tertiary structure falls apart.
  • Their may be a few bonds at various points which fold or bend this strucutre

Hydrogen bonds - weak and few off them

Hydrophobic bonds - weak and few of them

ionic bonds - weak and very few of them

Disulphide bonds - less easily broken than others (stronger) but very very few of them

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Quaternary Structure

  • Quaternary strucutre is a protein made up of 2 or more polypeptide chains
  • Its maintained by same sort of bonds as the tertiarry structure
  • Haemoglobin is an example of a protein with a quaternary strucutre

(http://t2.gstatic.com/images?q=tbn:ANd9GcSIEYo7g5hDFZ1HzMOZhqNA9JkaxGaRJJKrb4kdRYMyT2JajzMTaQ) different colours represent different chains

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Fiborous proteins

  • Make fibres (structural and muscle)
  • Not compact
  • Not soluble
  • Cannot make suspensions
  • Structiral fibres are mainly secondary structures but do not form tertiary structures

(http://www.google.co.uk/url?source=imglanding&ct=img&q=http://upload.wikimedia.org/wikipedia/commons/thumb/d/d1/Collagentriplehelix.png/79px-Collagentriplehelix.png&sa=X&ei=J4x0Ts-HHNGu8QP5rOWCDg&ved=0CAYQ8wc&usg=AFQjCNFrkHAW-t-LooxTghqgTkwDomYyfg)

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Globular Proteins

  • Globular proteins include enzymes,transport molecules, antibodies, hormones
  • Form compact rounded shape (hence the name globular)
  • Can form suspension ( they can move in and out of blood and be secreted in and out of cells)
  • Alll form tertiary structures

(http://t2.gstatic.com/images?q=tbn:ANd9GcQhO3wjnAc6rYsdWJ-Av5GkM_xYpixRG8f2KP0oTjlG83qyVMiC)

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