IT PROVIDES STRUCTURE IN MEMBRANES, BUILD CARTILAGE AND CONNECTIVE TISSUE, TRANSPORT OXYGEN IN BLOOD AND MUSCLE, DIRECT BIOLOGICAL REACTIONS AS ENZYMES, DEFEND THE BODY AGAINST INFECTION AND CONTROL METABOLIC PROCESSES AS HORMONES

(a)  

PROTEINS ARE LINEAR POLYMERS BUILT OF MONOMER UNITS CALLED

(a)  

WHAT TWO ELEMENTS PROVIDED BY PROTEIN ARE UNAVAILABLE FROM FATS AND CARBOHYDRATES, THE OTHER MAJOR CLASSES OF FOOD MOLECULES

(a)  

MOST PROTEINS IN AN ORGANISM ARE MADE FROM A SET OF _ STRUCTURALLY SIMILAR AMINO ACIDS

(a)  

THEY ARE THE BUILDING BLOCKS OF PROTEINS

(a)  

ALL 20 OF THE COMMON AMINO ACIDS ARE (a)  

WHAT ARE THE 4 SUBSTITUENTS OF AMINO ACIDS

(a)  

ALL AMINO ACIDS ISOLATED FROM PROTEINS HAVE THE GENERAL STRUCTURE EXCEPT FOR (a)  

AMINO ACIDS DIFFER FROM EACH OTHER IN THEIR _________ OR ________

(a)  

THE (a)   OF THE AMINO ACID IS A CHIRAL CENTER IN WHICH IT IS BONDED TO FOUR DIFFERENT GROUP

ALL OF THE AMINO ACIDS ARE CHIRAL AND OPTICALLY ACTIVE EXCEPT FOR (a)  

THE A-CARBON ATOM HAS A (a)   ARRANGEMENT OF THE BONDING ORBITALS AROUND IT

THE 4 DIFFERENT GROUPS OF AN A-CARBON ATOM CAN OCCUPY TWO UNIQUE (a)  

AMINO ACIDS HAVE 2 POSSIBLE (a)   , THE L AND D

ALL THE AMINO ACIDS IN ALL THE PROTEINS IN OUR BODY ARE (a)  

THEY ARE EXTREMELY RARE IN ANTURE; SOME ARE FOUND, FOR EXAMPLE, IN THE CELL WALLS OF A FEW TYPES OF BACTERIA

(a)  

IT IS DETERMINED BASED UPON COMPARISON OF AMINO ACIDS WITH D-GLYCERALDEHYDE

(a)  

THE POLARITY OF THE (a)   VARIES WIDELY, FROM NONPOLAR AND HYDROPHOBIC (WATER-INSOLUBLE) TO HIGHLY POLAR AND HYDROPHILIC (WATER-SOLUBLE)

THE R GROUPS IN THIS CLASS OF AMINO ACIDS ARE NONPOLAR AND HYDROPHILIC

(a)  

THE SIDE CHAINS OF _______,________,_______,________ TEND TO CLUSTER TOGETHER WITHIN PROTEINS, STABILIZING PROTEIN STRUCTURE BY MEANS OF HYDROPHOBIC INTERACTIONS

(a)  

IT HAS THE SIMPLEST STRUCTURE; ALTHOUGH IT IS MOST EASILY GROUPED WITH THE NONPOLAR AMINO ACIDS, ITS VERY SMALL SIDE CHAIN MAKES NO REAL CONTRIBUTION TO HYDROPHOBIC INTERACTIONS

(a)  

IT IS ONE OF THE TWO SULFUR-CONTAINING AMINO ACIDS, HAS A NONPOLAR THIOETHER GROUP IN ITS SIDE CHAIN

(a)  

IT HAS AN ALIPHATIC SIDE CHAIN WITH A DISTINCTIVE CYCLIC STRUCTURE

(a)  

THE SECONDARY AMINO (IMINO) GROUP OF ______ RESIDUES IS HELD IN A RIGID CONFORMATION THAT REDUCES THE STRUCTURAL FLEXIBILITY OF POLYPEPTIDE REGIONS CONTAINING ________

(a)  

PHENYLALANINE, TYROSINE, AND TRYPTOPHAN BELONG IN THIS R GROUP

(a)  

__________,_______ AND _________ ARE RELATIVELY NONPOLAR (HYDROPHOBIC) AND ALL CAN PARTICIPATE IN HYDROPHOBIC INTERACTIONS

(a)  

THE HYDROXYL GROUP OF (a)   CAN FORM HYDROGEN BONDS, AND IT IS IMPORTASNT FUNCTIONAL GROUP IN SOME ENZYMES

TYROSINE IS MORE POLAR THAN PHENYLALANINE BECAUSE OF ITS (a)  

TRYPTOPHAN IS MORE POLAR THAN PHENYLALANINE BECAUSE OF THE (a)  

THE R GROUPS IN THIS AMINO ACIDS ARE MORE SOLUBLE IN WATER, OR MORE HYDROPHILIC, THAN THOSE OF THE NONPOLAR AMINO ACIDS

(a)  

POLAR, UNCHARGED R GROUP CLASS OF AMINO ACIDS INCLUDES ______,______,_______, ________ AND _______

(a)  

THE POLARITY OF _________ AND ________ IS CONTRIBUTED BY THEIR HYDROXYL GROUP

(a)  

THE POLARITY OF (a)   IS CONTRIBUTED BY ITS SULFHYDRYL GROUP

THE POLARITY OF _________ AND ________ IS CONTRIBUTED BY THEIR AMIDE GROUP

(a)  

IT IS READILY OXIDIZED TO FORM A COVALENTLY LINKED DIMERIC AMINO ACID CALLED CYSTINE

(a)  

IT IS TWO CYSTEINE MOLECULES OR RESIDUES JOINED TOGETHER BY A DISULFIDE BOND

(a)  

THEY PLAY A SPECIAL ROLE IN THE STRUCTURES OF MANY PROTEINS BY FORMING COVALENT LINKS BETWEEN PARTS OF A POLYPEPTIDE MOLECULE OR BETWEEN TWO DIFFERENT POLYPEPTIDE CHAINS

(a)  

LYSINE, ARGININE, AND HISTIDINE BELONG IN THIS R GROUP

(a)  

THE AMINO ACIDS IN WHICH THE R GROUPS HAVE SIGNIFICANT POSITIVE CHARGE AT pH 7.0 ARE ________,_________, ________

(a)  

IT HAS A SECOND PRIMARY AMINO GROUP AT THE E POSITION ON ITS ALIPHATIC CHAIN

(a)  

IT HAS A POSITIVELY CHARGED GUANIDINIUM GROUP

(a)  

IT HAS AN AROMATIC IMIDAZOLE GROUP

(a)  

ALL 20 AMINO ACIDS ARE NEEDED TO MAKE PROTEINS BUT OUR BODY CAN SYNTHESIZE ONLY _

(a)  

WHAT ARE THE 10 ESSENTIAL AMINO ACIDS

(a)  

OBTAINED FROM ANIMAL SOURCES SUCH AS MEAT, POULTRY, EGGS, DAIRY AND FISH

(a)  

IT IS OBTAINED FROM VEGETABLE SOURCES

(a)  

WHICH AMINO ACIDS ARE LOW IN INCOMPLETE PROTEIN

(a)  

AMINO ACID DEFICIENCY IN GELATIN

(a)  

AMINO ACID DEFICIENCY IN WHEAT

(a)  

AMINO ACID DEFICIENCY IN CORN

(a)  

AMINO ACID DEFICIENCY IN RICE (BROWN, WHITE)

(a)  

AMINO ACID DEFICIENCY IN OATS

(a)  

AMINO ACID DEFICIENCY IN BEANS

(a)  

AMINO ACID DEFICIENCY IN PEAS

(a)  

AMINO ACID DEFICIENCY IN ALMOND

(a)  

AMINO ACID DEFICIENCY IN WALNUTS

(a)  

ALL 20 AMINO ACIDS THAT ARE FOUND IN PROTEINS ARE (a)  

THESE ARE RESIDUES THAT HAVE BEEN CHEMICALLY MODIFIES AFTER THEY HAVE BEEN INCORPORATED INTO A POLYPEPTIDE AND ALSO AMINO ACIDS THAT OCCUR IN LIVING ORGANISMS BUT ARE NOT FOUND IN PROTEINS

(a)  

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EXAMPLE OF MODIFIED AMINO ACID RESIDUES WHICH IS AN IMPORTANT STRUCTURAL CONSTITUENTS OF THE FIBROUS PROTEIN COLLAGEN AND THE MOST ABUNDANT PROTEIN IN MAMMALS

(a)  

EXAMPLE OF MODIFIED AMINO ACID RESIDUES WHICH IS AN IMPORTANT STRUCTURAL CONSTITUENTS OF THE FIBROUS PROTEIN COLLAGEN AND THE MOST ABUNDANT PROTEIN IN MAMMALS

(a)  

CONSTITUENT OF SEVERAL PROTEINS INVOLVED IN BLOOD CLOTTING

(a)  

(a)  

PRESENCE OF P REGULATES THE ACTIVITY OF PROTEINS

(a)  

(a)  

IT IS MADE UP OF TWO CYSTEINE MOLECULES OR RESIDUES JOINED TOGETHER BY A DISULFIDE BOND

(a)  

THEY PLAY A SPECIAL ROLE IN THE STRUCTURES OF MANY PROTEINS BY FORMING COVALENT CROSS-LINKS

(a)  

A METABOLITE OF THE UREA CYCLE

(a)  

A METABOLITE OF THE UREA CYCLE

(a)  

WHEN AN AMINO ACID LACKING AN IONIZABLE R GROUP IS DISSOLVED IN WATER AT NEUTRAL pH, IT EXISTS IN A SOLUTION AS THE DIPOLAR ION, OR (a)  

THE (a)   DOES NOT OCCUR IN SIGNIFICANT AMOUNTS OF AQUEOUS SOLUTIONS

IT PREDOMINATES AT NEUTRAL pH

(a)  

THE ZWITTERION FORM OF AN AMINO ACID EXISTS AT A pH VALUE IS CALLED

(a)  

THEY HAVE ISOELECTRIC POINTS AT pH VALUES CLOSE TO 7

(a)  

THEY HAVE ISOELECTRIC POINTS AT MUCH HIGHER pH VALUES

(a)  

THEY BECOME ELECTRICALLY NEUTRAL AT LOW pH VALUES

(a)  

AT pH VALUES BELOW OR ABOVE THEIR ISOELECTRIC POINTS, ZWITTERIONS ACT AS ACIDS AND BASES BECAUSE THEY ARE ABLE TO DONATE OR ACCEPT (a)  

SUBTAANCES HAVING DUAL (ACID-BASE) NATURE ARE OFTEN CALLED

(a)  

BECAUSE AMINO ACIDS CONTAIN (a)   THE PREDOMINANT IONIC FORM OF THESE MOLECULES IN SOLUTION DEPENDS ON THE pH

IT ILLUSTRATES THE EFFECT OF pH ON AMINO ACID STRUCTURE

(a)  

BECAUSE THERE IS NO NET CHARGE AT THE ISOELECTRIC POINT --- AMINO ACIDS ARE (a)   AT THIS pH

AMINO ACIDS WITH (a)   HAVE MORE COMPLEX TITRATION CURVES

THE pka AND THE pl VALUES OF AMINO ACIDS IN PEPTIDES AND PROTEINS DIFFER SOMEWHAT FROM THOSE OF FREE AMINO ACIDS, PRINCIPALLY BECAUSE MOST OF THE A-AMINO AND A-CARBOXYL GROUPS ARE NOT IONIZED BUT ARE COVALENTLY JOINED IN (a)  

A CHAIN OF AMINO ACIDS HELD TOGETHER BY PEPTIDE BONDS OR AMIDE BONDS

(a)  

IT OCCURS BETWEEN THE CARBOXYL GROUP OF ONE AMINO ACID AND THE AMINO GROUP OF THE NEXT WITH THE LOSS OF WATER

(a)  

TWO AMINO ACIDS FORM A

(a)  

THREE AMINO ACIDS FORM A

(a)  

FOUR AMINO ACIDS FORM A

(a)  

LONG CHAINS OF AMINO ACIDS ARE CALLED

(a)  

THE REPEATING CHAIN OF AMIDE LINKAGES

(a)  

THE NAMES OF ALL THE OTHER AMINO ACIDS IN A PEPTIDE END WITH YL, EXCEPT FOR THE (a)   AMINO ACID

AN AMINO ACID POLYMER OF SHORT CHAIN LENGTH

(a)  

AN AMINO ACID POLYMER OF INTERMEDIATE CHAN LENGTH CONTAINING UP TO 50 AMINO ACID RESIDUES

(a)  

AN AMINO ACID POLYMER MADE UP OF MORE THAN 50 AMINO ACIDS

(a)  

AN AMINO ACID THAT IS A PART OF A PEPTIDE, POLYPEPTIDE, OR PROTEIN CHAIN

(a)  

AN AMINO ACID ON THE END OF A CHAIN THAT AS AN UNREACTED OR FREE AMINO GROUP

(a)  

AN AMINO ACID ON THE END OF A CHAIN THAT HAS AN UNREACTED OR FREE CARBOXYLATE GROUP

(a)  

their structures are less complex than the larger protein molecules

(a)  

A TRIPEPTIDE THAT CONTAINS AN UNUSUAL Y-AMIDE GROUP;

IS FOUND IN ALMOST ALL ORGANISMS;

IS INVOLVED IN MANY IMPORTANT BIOLOGICAL PROCESSES;

IT PROTECTS CELLS FROM THE DESTRUCTIVE EFFECTS OF OXIDATION BY REACTING WITH SUBSTANCES SUCH AS PEROXIDES ;

(a)