Chapter 20 - Biochemistry

Covalent bonds

Covalent bonds

________ produce tissues that are hard and less flexible.

Catalysts

(enzymes) speeds up reversible reaction in both directions.

Biocatalysis

use of enzymes to catalyze chemical reactions run in industrial- sized reactors.

Α helix

________: coiled arrangement with R groups pointing outwards.

Primary

________ (first degree) structure: sequence of amino acids starting with the N- terminus.

Quaternary

________ (fourth degree) structure: larger structure functioning as a single unit that results when two or more proteins associate.

Peptides

________: shortest chains, only a few amino acids long.

Higher turnover

________ number results in a faster enzyme- catalyzed reaction.

Polypeptides

________: more than twenty amino acid residues.

Oligopeptides

________: up to twenty amino acid residues.

Dextrorotary

________ and levorotary enantiomers are designated with (+) and-) (signs according to optical properties.

Tertiary

________ (third degree) structure: three- dimensional biologically active structure of protein that arises because of interactions between R groups on amino acids.

Enzymes

________: proteins that are biological catalysts.

Zwitterions

________: describes molecules that contain positive and negatively charged functional groups even when its a neutral molecule.

Deprotonates

________: alanine loses a hydrogen from its- NH3+ group to form an- NH2 group.

Anabolism

________: synthesis of complex materials from simple feedstocks.

Inhibitors

________: compounds that diminish or destroy effectiveness of enzymes.

Α carbon groups

chiral centers because the generic structure of an amino acid is bonded to four different groups

Proteins

most abundant class of biomolecules in all animals; major component for various tissues, enzymes, molecules and hormones that contribute to biological function

Essential Amino Acids

10 amino acids that must be present in what we eat, marked with subscript b

Amino acid enantiomers

designated by prefixes (D- dextro, right and l- levo, left), pertains to how the chiral atom is oriented in space.

Active sites

bind reactant molecules, called substrates, held in site by intermolecular interactions.

Amino Acids

building blocks of proteins; named because they each contain at least one amine (-NH2) group and carboxylic acid (-COOH) group

R Group

generally highlighted in pink, often called side-chain groups

Essential Amino Acids

10 amino acids that must be present in what we eat, marked with subscript b

Zwitterions

describes molecules that contain positive and negatively charged functional groups even when its a neutral molecule

Deprotonates

alanine loses a hydrogen from its -NH3+ group to form an -NH2 group

Peptides

shortest chains, only a few amino acids long

dipeptides

two amino acid residues

tripeptides

three amino acid residues

oligopeptides

up to twenty amino acid residues

polypeptides

more than twenty amino acid residues

peptide bond

bond linking the amino acids in peptides and proteins, forms when the α-carboxylic group of one amino acid reacts with the α-amine group of another

amine (N-) terminus

left end

carboxylic acid (C-) terminus

right end

Primary (first degree) structure

sequence of amino acids starting with the N-terminus

Secondary (secondary degree) structure

first stage of folding process, pattern of arrangement of segments in a protein chain; reflects hydrophobic interactions and intermolecular forces

α helix

coiled arrangement with R groups pointing outwards

Tertiary (third degree) structure

three-dimensional biologically active structure of protein that arises because of interactions between R groups on amino acids

formed by intermolecular forces and covalent bonds

specifically disulfide bonds

Quaternary (fourth degree) structure

larger structure functioning as a single unit that results when two or more proteins associate

Enzymes

proteins that are biological catalysts

catabolism

breakdown of molecules

anabolism

synthesis of complex materials from simple feedstocks

biocatalysis

use of enzymes to catalyze chemical reactions run in industrial-sized reactors

active sites

bind reactant molecules, called substrates, held in site by intermolecular interactions

inhibitors

compounds that diminish or destroy effectiveness of enzymes