AMINO ACIDS

EXAMPLES OF AMINO ACIDS THAT ARE ALIPHATIC AND IS NON POLAR

GLYCINE AND ALANINE

EXAMPLES OF AMINO ACIDS THAT ARE BRANCHED AND IS NON-POLAR

LEUCINE, ISOLEUCINE, VALINE, PROLINE, METHIONINE

EXAMPLES OF AMINO ACIDS THAT ARE AROMATIC AND NON-POLAR

PHENYLALANINE AND TRYPTOPHAN

EXAMPLES OF AMINO ACIDS THAT ARE AROMATIC AND POLAR

TYROSINE (HYDROXYL)

EXAMPLES OF AMINO ACIDS THAT ARE UNCHARGED AND POLAR

HYDROXYL (SERINE AND THREONINE), AMIDE (GLUTAMINE AND ASPARAGINE), SULFHYDRYL (CYSTEINE)

EXAMPLES OF AMINO ACIDS THAT ARE POSITIVELY CHARGED AND POLAR

HISTIDINE, LYSINE, ARGININE

EXAMPLES OF AMINO ACIDS THAT ARE NEGATIVELY CHARGED AND POLAR

ASPARTATE AND GLUTAMATE

THIS DO NOT BIND NOR GIVE OFF PROTONS (INERT); DO NOT PARTICIPATE IN HYDROGEN BONDS OR IONIC BONDS

AMINO ACID WITH NON-POLAR SIDE CHAIN

THIS INTERACT POORLY WITH WATER; THEY ARE HYDROPHOBIC OR WATER FEARING SUBSTANCES IN NATURE

AMINO ACIDS WITH NON-POLAR SIDE CHAINS

SIDE CHAINS OF AMINO ACIDS (NON-POLAR) CAN BE THOUGH OF AS ____, WHICH PROMOTES HYDROPHOBIC INTERACTIONS

OILY OR LIPID LIKE

THEY PLAY AN IMPORTANT ROLE IN MAINTAINING THE CONFORMATION OF 3-DIMENSIONAL STRUCTURE OF PROTEINS

AMINO ACIDS WITH NON-POLAR SIDE CHAINS

AMINO ACIDS WITH A LINEAR SIDE CHAIN

AMINO ACID WITH ALIPHATIC SIDE CHAIN (GLYCINE AND ALANINE)

THIS IS THE SIMPLEST AMINO ACID AND ONLY AMINO ACID WITHOUT CHIRALITY (NO CHIRAL/ASYMMETRIC CARBON)

GLYCINE

THE STRUCTURE OF THIS AMINO ACID HAS A HYDROGEN SIDE CHAIN

GLYCINE

THE STRUCTURE OF THIS AMINO ACID HAS A METHYL GROUP SIDE CHAIN

ALANINE

BULKY AMINO ACIDS BECAUSE OF THEIR R GROUPS

BRANCHED CHAIN AMINO ACIDS

THE SECOND CARBON ATTACHED TO IT IS THE BETA CARBON THAT CONTAINS TWO METHYL GROUP

VALINE

GAMMA CARBON THAT CONTAINS TWO METHYL GROUPS

LEUCINE

THIS MEANS CHANGING LOCATIONS OF SOME FUNCTIONAL GROUPS

ISO

BETA CARBON CONTAINS METHYL GROUP ISOMER OF LEUCINE

ISOLEUCINE

A METHYL GROUP; ONE OF THE SULFUR-CONTAINING AMINO ACIDS

METHIONINE

METHIONINE BECOMES FUNCTIONAL WHEN CONVERTED TO?

S-ADENOSYLMETHIONINE (SAM)

ACTIVATED FORM OF METHIONINE

S-ADENOSYLMETHIONINE

METHYL GROUP DONOR IN METHYLATION REACTIONS

S-ADENOSYLMETHIONINE

THIS IS UNIQUE BECAUSE ITS SIDE CHAIN ATTACHES TO THE ALPHA AMINO NITROGEN SO IT FORMS A RING STRUCTURE

PROLINE

IN PROLINE, A RING STRUCTURE IS FORMED WHICH IS CALLED AN?

ALPHA-IMINO STRUCTURE

SIDE CHAIN AND ALPHA AMINO GROUP FORM A RING STRUCTURE (IMINO RING)

PROLINE

ALSO KNOWN AS THE A-HELIX BREAKER. WHEN YOU CONNECT IT TO THE HELICAL STRUCTURE OF PROTEINS IT COULD CREATE A KINK, WHICH COULD BREAK THE A-HELICAL STRUCTURE

PROLINE

ALPHA AMINO NITROGEN TO FORM RING STRUCTURE

PROLINE

THIS MEANS AN AMINO ACID CONTAINS A RING STRUCTURE IN THEIR SIDE CHAIN

AROMATIC

AMINO ACID THAT MAY EITHER BE STRAIGHT OR BRANCHED; PROPERTY OF BEING HYDROPHOBIC OR NON POLAR

ALIPATHIC

BENZENE RING/PHENYL RING SIDE CHAIN

PHENYLALANINE

PRECURSOR OF TYROSINE

PHENYLALANINE

AROMATIC NONPOLAR; RING STRUCTURE BUT UNDER HYDROXYL AMINO ACIDS

PHENYLALANINE

WHEN THE SIDE CHAIN OF PHENYLALANINE IS CONVERTED TO TYROSINE, JUST ADD _____ TO BECOME HYDROXYLATED

OH GROUP

THIS HAS 2 RING STRUCTURES, INDOLE RING, NITROGEN SIDE CHAIN

TRYPTOPHAN

THESE AMINO ACIDS HAVE ZERO NET CHARGE AND ARE AT A NEUTRAL PH

AMINO ACID WITH UNCHARGED POLAR GROUP

THIS PROPERTY IS AN IMPORTANT FACTOR IN PROTEIN STRUCTURE

HYDROPHILIC PROPERTY

WHAT ARE UNDER HYDROXYL-CONTAINING AMINO ACIDS?

SERINE, THREONINE, TYROSINE

SITE OF PHOSPHORYLATION REACTION (ONE WAY OF ACTIVATING OR INACTIVATING ENZYMES); ENZYMES ARE PROTEINS; REGULATE ENZYME ACTIVITY; SITE OF GLYCOSYLATION REACTION (ADDITION OF SUGARS OR OLIGOSACCHARIDE UNITS)

HYDROXYL-CONTAINING AMINO ACIDS

ON ITS SIDE CHAIN, THE BETA CARBON HAD THE HYDROXYL (-OH) GROUP

SERINE

THE SIDE CHAIN HAS HYDROXYL AND METHYL GROUP

THREONINE

DERIVED FROM PHENYLALANINE, ATTACHMENT OF HYDROXYL IN THE RING STRUCTURE

TYROSINE

THESE ARE IMPORTANT IN AMMONIA DETOXIFICATION

GLUTAMINE AND ASPARAGINE

PRIMARY SOURCE OF URINARY AMMONIA. CAN ACT AS CARRIER OF EXTRA AMIDE NITROGEN AND CAN GO TO THE RENAL SYSTEM WHERE IT IS EXCRETED

GLUTAMINE

ON THE BETA CARBON THERE IS A SIDE CHAIN CARBOXYL GROUP (C=O) AND SIDE CHAIN AMIDE GROUP (NH2)

ASPARAGINE

SIDE CHAIN IS SHORTER

A. ASPARAGINE

B. GLUTAMINE

C. BOTH

D. NEITHER

A

THAT HAS EXTRA CARBON. IT HAS ALPHA, BETA, GAMMA CARBON WHERE IT CONTAINS SIDE CHAIN CARBOXYL AND AMIDE GROUP

GLUTAMINE

THIS ALSO CONTAIN SULFUR ON ITS SIDE CHAIN

CYSTEINE

2ND AMINO ACID WITH SULFUR ON ITS SIDE CHAIN

CYSTEINE

ITS SIDE CHAIN IS THIO GROUP OR SOCHOIDRAL GROUP OR THIOALCOHOL GROUP

CYSTEINE

CONTAINS THE SULFHYDRYL (-SH) GROUP/THIOL GROUP

CYSTEINE

WHEN TWO CYSTEINE RESIDUES COMBINE WITH A STRONG DISULFIDE BOND, WHAT IS THE RESULTING PRODUCT?

CYSTINE

THIS IS SEEN IN SOME PEPTIDES WHEN THEY ARE LINKED TOGETHER BY A DISULFIDE BOND

DIMER CYSTINE

THIS BOND IS ALSO IMPORTANT IN MAINTENANCE OF PROTEIN STRUCTURE; ALSO IMPORTANT IN THE 3-DIMENSIONAL STRUCTURE OF YOUR PROTEIN

DISULFIDE BOND

THIS WORKS BY BLOCKING THE RELEASE OF ACETYLCHOLINE

BOTULINUM TOXIN

PLAYS A KEY PART IN THE WAY THAT NERVES STIMULATE MUSCLES TO CONTRACT

ACETYLCHOLINE

THIS CONTAINS IMIDAZOLE GROUP ON ITS SIDE CHAIN

HISTIDINE

THIS IS RESPONSIBLE ALSO FOR THE BUFFERING CAPACITY OF HEMOGLOBIN

HISTIDINE

THIS CONTAINS GUANIDO GROUP OR GUANIDINO GROUP

ARGININE

HOW MANY NITROGEN DOES LYSINE HAVE?

1 NITROGEN

HOW MANY NITROGEN DOES ARGININE HAVE?

3 NITROGEN

HOW MANY NITROGEN DOES HISTIDINE HAVE?

3 NITROGEN ON RING STRUCTURE

THERE ARE THREE SIDE CHAINS, THE ATTACHMENT OF THE FIRST NITROGEN IS AT THE GAMMA CARBON AND THERE IS ANOTHER CARBON AT THE SIDE CHAIN

ARGININE

THE SIDE CHAIN OF ARGININE IS CALLED?

GUANIDINO GROUP

THIS IS ALSO THE PRECURSOR OF UREA, WHICH IS A COMPONENT OF LOTION TO TREAT DRY SKIN (CAUSED BY DIABETES), SCHEMA, AND PSORIASIS

ARGININE

IT HAS A RING STRUCTURE, CAN ALSO BE INCLUDED IN THE AROMATIC AMINO ACID; THERE ARE TWO SIDE CHAINS, CALLED IMIDAZOLE GROUP AND IT HAS 2 EXTRA NITROGEN IN SIDE CHAINS

HISTIDINE

THEY HAVE LENGTHY/HEAVY SIDE CHAINS; THEY HEAVY SIDE CHAINS AFFECT THE 3-D STRUCTURES

HISTIDINE, LYSINE, ARGININE

IN STABILIZATION OF PROTEINS, ONE OF THE REASONS WHY SOME PROTEINS BECOME UNSTABLE, ITS BECAUSE OF THEIR?

LENGTHY SIDE CHAINS

ACIDIC SIDE CHAIN AMINO ACIDS

AMINO ACIDS WITH NEGATIVELY CHARGED GROUP

Y (GAMMA) CARBON WITH THE CARBOXYL GROUP; LONGER SIDE CHAINS

GLUTAMIC ACID

B (BETA) CARBON WITH THE CARBOXYL GROUP; SHORTER SIDE CHAINS

ASPARTIC ACID

INTERACTIONS BETWEEN ACIDIC AND BASIC AMINO ACIDS RESULTS IN THE FORMATION OF?

IONIC BOND

THIS IS IMPORTANT IN MAINTAINING PROTEIN STRUCTURE

AMINO ACIDS WITH NEGATIVELY CHARGED GROUP

PROTON DONORS

AMINO ACID WITH NEGATIVELY CHARGED GROUPS

WHAT IS 21ST AMINO ACID?

SELENOCYSTEINE

SYNTHESIZED FROM SERINE AND SELENIUM

SELENOCYSTEINE

FOUND IN PROTEINS SUCH AS GLUTATHIONE PEROXIDASE, DEIODINASES, AND THIORADOXIN REDUCTASE

SELENOCYSTEINE

CYSTEINE ANALOGUE

SELENOCYSTEINE

SELENIUM-CONTAINING SELENOL GROUP IN PLACE OF SULFUR CONTAINING THIOL GROUP

SELENOCYSTEINE

22ND AMINO ACID

PYRROLYSINE

THE STOP CODON UAG CAN CODE FOR?

PYRROLYSINE

GENETICALLY CODED AMINO ACID USED BY SOME METHANOGENIC ARCHAEA AND ONE KNOWN BACTERIUM

PYRROLYSINE

USED IN ENZYME THAT ARE PART OF METHANE-PRODUCING METABOLISM

PYRROLYSINE

SIMILAR TO LYSINE, BUT WITH ADDED PYRROLINE RING LINKED TO THE END OF THE LYSINE SIDE CHAIN

PYRROLYSINE

AMINO ACIDS ARE SOLUBLE IN POLAR SOLVENTS SUCH AS?

WATER AND ETHANOL

AMINO ACIDS ARE INSOLUBLE IN NONPOLAR SOLVENTS SUCH AS?

BENZENE, HEXANE, OR ETHER

AMINO ACID HAVE (HIGH, LOW) MELTING POINTS

HIGH

MELTING POINT OF AMINO ACIDS

MORE THAN 200C

A TEMPERATURE HIGHER THAN 100C WILL ____ THE SKIN

DESSICATE

FOR ALL THE STANDARD AMINO ACIDS, EXCEPT _____, THE A-CARBON IS ASYMMETRIC, BONDED TO FOUR DIFFERENT SUBSTITUENT GROUPS. IN THIS CASE THE A-CARBON IS CHIRAL CENTER

GLYCINE

GLYCINE IS AN EXCEPTION TO A-CARBON CHIRAL CENTER BECAUSE IT HAS A ____ ON ITS SIDE CHAIN

HYDROGEN

ALL MOLECULES WITH A CHIRAL CENTER ARE ____, THEY CAN ROTATE THE PLANE POLARIZED LIFHT EITHER TO THE RIGHT OR TO THE LEFT

OPTICALLY ACTIVE

AMINO ACID THAT OCCUR IN PROTEIN ARE ALL IN WHAT FORM?

L FORM

THESE ARE FOUND IN BACTERIAL CELL WALLS AND SOME ANTIBIOTICS

D-AMINO ACID

WHAT ARE THE TWO D-AMINO ACIDS THAT ARE FOUND IN THE HUMAN BRAIN

D-ASPARTATE AND D-SERINE

ULTRAVIOLET ABSORPTION PROPERTIES OF PROTEINS ARE DETERMINED SOLELY BY?

PHENYLALANINE, TYROSINE, TRYPTOPHAN

AMINO ACIDS ARE COLORLESS EXCEPT FOR?

AROMATIC AMINO ACIDS

UAS US ABLE TO ABSORB UV WAVELENGTHS DUE TO THEIR?

AROMATICITY (250 TO 290NM)

TRYPTOPHAN CAN BE ABSORB WAVELENGTHS OF AROUND ___

290NM