classify protein according to its function:
hemoglobin, oxygen carrier in the blood

transport

classify protein according to its function:
collagen, a major component of tendons and cartilage

structural

classify protein according to its function:
keratin, a protein found in hair

structural

classify protein according to its function:
amylases that hydrolyze starch

enzyme

classify protein according to its function:
insulin, a protein needed for glucose utilization

hormone

classify protein according to its function:
antibodies, proteins that disable foreign proteins

protection

classify protein according to its function:
casein, milk protein

storage

classify protein according to its function:
lipases that hydrolyze lipids

enzyme

what functional groups are found in all alpha amino acids

carboxylic acid an amino group

protein that consists of long, thin, fiber like shapes.

fibrous

proteins that make up structural tissues such as hair, wool, skin and nails

fibrous

proteins that have spherical shapes

globular

proteins that carry out the functions of the cells such as synthesis, transport and metabolism

globular

found in eggs, milk, meat, fish an poultry

essential amino acids

R is hydrocarbon or aromatic

nonpolar

hydrophobic

nonpolar

R contains polar molecule such as OH

polar

hydrophilic

polar

R contains COOH group

acidic

R contains NH2 group

basic

during ionization of amino acid the COOH group donates or accepts a proton?

donates

during ionization of amino acid the NH2 donates or accepts a proton

accepts

In solutions near neutral pH, most amino acids exist in the ionized form called the

Zwitterion

the Zwitterion has a net charge of

zero

in basic solutions the NH3 donates a proton thus forming an ion with a positive or negative charge?

negative

in acidic solutions the COO- accepts a proton thus forming a ion with a positive or negative charge

positive

in acidic solutions the COO- accepts or donates a proton

accepts

in acidic solutions the NH3 accepts or donates a proton

donates

peptide bonds can be broken by

hydrolysis

secondary structure is determined by

the amino acid sequence, the primary structure

folding of the primary structure into a specific shape

secondary structure

held together by H bonds between N-H and C=O

secondary structure

three main secondary structures shapes

alpha helix, beta pleated sheets and triple helix

coil with H bonds between N-H group and O of a C=O in the next turn

alpha helix

polypeptides held together side by side by H bonds to make sheets

beta pleated sheet

fibrous proteins such as silk

beta pleated sheet

hydrogen bonds form between oxygen atoms in the carbonyl groups of one polypeptide chain and the hydrogen atoms in the N-H groups of the amide bonds

beta pleated sheet

three polypeptide chains woven together like a braid

triple helix

held together by H bonds such as collagen

triple helix

most abundant protein in the body

collagen

located in fibrous proteins such as wool and hair

tertiary structure

helical chains coil together to form a structure like a rope and are held together by S-S bonds

tertiary structure

most proteins in the body are made what kind of proteins

globular

insulin, hemoglobin, enzymes and antibodies are all what kind of proteins

globular

proteins made of polypeptide chains that are folded into different secondary structures that are in turn folded into tertiary structure

globular

the tertiary structure of most globular proteins is the active or inactive form

active

the globular protein that stores oxygen in skeletal muscles

myoglobin

primary structure consists of polypeptide of 153 amino acids

myoglobin

tertiary structure is compact shape due to the folding of molecule to form a pocket for O2 to bind

myoglobin

the molecule is active only in its tertiary structure

myoglobin

tis formed when a globular protein is made of 2 or more peptide chains

quaternary structure

the peptide chains can be similar or different and are folded into its secondary and tertiary structure

quaternary structure

formed by the binding of the polypeptides in their tertiary structures together

quaternary structure

globular protein that transports oxygen to the blood

hemoglobin

protein that consists of 4 polypeptide chains or subunits

hemoglobin

how should the 4 subunits be held together in hemoglobin

by four different bonds like H bonds and S-S bonds in the quaternary structure

bond type of:
primary

peptide

bond type of:
secondary

H bonds

bond type of:
tertiary

H bonds and S-S bonds

bond type of:
quaternary

H bonds and S-S bonds

proteins in the primary and secondary structure are active or inactive?

inactive

proteins in the tertiary are active if

only one polypeptide is needed

proteins in the tertiary are inactive if

more than one polypeptide is needed

proteins in the quaternary structure are

active

the sequence of amino acids

primary

the coiled alpha helix, beta pleated sheet, or a triple helix formed by hydrogen bonding between peptide bonds along the chain

secondary

a folding of the protein into a compact, three dimensional shape stabilized by interactions between side R groups of amino acids

tertiary

a combination of two or more protein subunits to form a larger biologically active protein

quaternary

occurs when the bonds that stabilizes the secondary, tertiary or quaternary are disrupted

denaturation

a denatured protein is active or inactive?

inactive

denaturation agents

heat (above 50c)
acids and bases disrupt bonds
organic compounds
heavy metal ions
agitation

globular proteins that catalyze chemical reactions in the body

enzymes

active site is rigid

lock and key model

active site is flexible

induced fit model

factors affecting enzyme action

substrate concentration
temperature
pH