m2 biological molecules

draw molecules of water with the hydrogen bonding between it and what type of bonding are the darker lines

how does a hydrogen bond form

hydrogen bonds form when a slightly negatively oxygen of one molecule comes close to a slightly positively charged hydrogen in another molecule

describe how water has a high boiling point

• a lot of energy needed to break hydrogen bonds

• creates stable water temp for aquatic animals

• less energy spent on temp control

describe how ice is less dense than water

• creates insulating barrier

• water below doesn’t freeze

• allowing organisms to move under water

• creates habitat for animals

describe cohesion and adhesion in water

• cohesion happens through hydrogen bonding in water and creates high surface tension for insects

• adhesion happens through attraction of water molecules to other surfaces

describe how water acts as a solvent

allows mineral ions to be transported around plants and animals

describe how water acts as a transport medium

allows transport of soluble substances

describe how water acts as a coolant

from evaporation and takes heat away from body

describe how water has high specific heat capacity

• takes a lot of energy to heat up water by one degrees

• creates stable temp

• enzymes can work at their optimum temp ,

• gases can remain soluble for aquatic organisms

describe how water has high latent heat of vaporisation

• takes a lot of energy to change water from liquid to gas form

• important for metabolic reactions

describe capillary action in water

allows water to move up narrow vessels

what’s a condensation reaction

when water is removed to form covalent bond

what’s a hydrolysis reaction

when water is added to break covalent bond

what elements are in the molecules carbohydrates,lipids,proteins,nucleic acids

• C H O for carbohydrates

• C H O for lipids

• C H O N S for proteins

• C H O N P for nucleic acids

what’s a monomer and polymer

• monomer is a single unit

• polymer is several monomers joined together

draw and state the difference between alpha glucose and beta glucose

the difference is the OH and H side on the carbon 1 right hand side have switched sides

describe features of glucose

• glucose is a hexose sugar it contains 6 carbon atoms

• glucose is a reducing sugar , when it is in solution it can reduce other chemicals

draw ribose

state which monosoccharides join to make each disaccharide maltose,lactose and sucrose

• alpha glucose+alpha glucose=maltose

• beta glucose+galactose=lactose

• alpha glucose+fructose=sucrose

describe structure and function starch including amylose and amylopectin

• mixture of amylose and amylopectin , both insoluble so doesn’t affect water potential , holds glucose in chains so it can easily be broken off from ends and used as glucose for respiration

• amylose has alpha 1 4 glycosidic bonds which create a coiled structure  , compact good for storage ,

• amylopectin alpha 1 4 and alpha 1 6 glycosidic bonds , created branched structure , allows hydrolysis of the ends by enzyme to create monosaccharides available for aerobic respiration

describe structure and function of glycogen

• made of alpha 1 4 and 1 6 glycosidic bonds

• insoluble , compact , doesn’t affect et water potential

• many ends so hydrolyse by enzymes to create aloha glucose again available for respiration

describe structure and function of cellulose

• beta glucose , beta 1 4 glycosidic bonds to make long chain

• form beta pleated sheets between which hydrogen bonds form cross links to form bundles called microforms , larger bundles called macrofibrils

• provides high tensile strength ,prevents cell from bursting , doesn’t affect water potential

draw amino acid structure

what’s a dipeptide

a dipeptide is two amino acids joining together to form a dipeptide

primary structure of proteins

• sequence of amino acids bonded by peptide bonds

secondary structure of proteins

• folding of polypeptide chain

• held in place with hydrogen bonds

• either alpha helix or beta pleated sheets

tertiary structure of proteins

• further folding of polypeptide chains

• held in place with hydrogen bonds , disulphide bridges , ionic bonds

• amino acids with hydrophobic R groups orientate towards center of protein

• hydrophilic r groups will orientate toward  outside of protein

quartenary structure of proteins

more than one polypeptide chain

describe fibrous proteins

• provide structural role

• insoluble in water ( lots of amino acids with hydrophobic R groups )

• very strong and tough ( many cross bridges between polypeptide chains )

give examples of fibrous proteins