Chemistry: Chapter 16 Flashcards

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

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

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

classify protein according to its function:
amylases that hydrolyze starch

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

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

classify protein according to its function:
casein, milk protein

classify protein according to its function:
lipases that hydrolyze lipids

what functional groups are found in all alpha amino acids

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

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

proteins that have spherical shapes

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

found in eggs, milk, meat, fish an poultry

R is hydrocarbon or aromatic

hydrophobic

R contains polar molecule such as OH

hydrophilic

R contains COOH group

R contains NH2 group

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

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

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

the Zwitterion has a net charge of

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

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

in acidic solutions the COO- accepts or donates a proton

in acidic solutions the NH3 accepts or donates a proton

peptide bonds can be broken by

secondary structure is determined by

folding of the primary structure into a specific shape

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

three main secondary structures shapes

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

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

fibrous proteins such as silk

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

three polypeptide chains woven together like a braid

held together by H bonds such as collagen

most abundant protein in the body

located in fibrous proteins such as wool and hair

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

most proteins in the body are made what kind of proteins

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

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

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

the globular protein that stores oxygen in skeletal muscles

primary structure consists of polypeptide of 153 amino acids

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

the molecule is active only in its tertiary structure

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

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

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

globular protein that transports oxygen to the blood

protein that consists of 4 polypeptide chains or subunits

how should the 4 subunits be held together in hemoglobin

bond type of:
primary

bond type of:
secondary

bond type of:
tertiary

bond type of:
quaternary

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

proteins in the tertiary are active if

proteins in the tertiary are inactive if

proteins in the quaternary structure are

the sequence of amino acids

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

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

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

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

a denatured protein is active or inactive?

denaturation agents

globular proteins that catalyze chemical reactions in the body

active site is rigid

active site is flexible

factors affecting enzyme action