PROTEINS 2

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Last updated 7:35 AM on 9/1/26
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137 Terms

1
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COMPLEX, ORGANIC NITROGENOUS SUBSTANCES WITH VERY HIGH MOLECULAR WEIGHTS, FOUND IN ALL PLANT AND ANIMAL CELLS, CONSISTING LARGELY OR ENTIRELY OF ALPHA AMINO ACIDS UNITED IN PEPTIDE LINKAGE

PROTEINS

2
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EXCITATORY NEUROTRANSMITTERS ARE?

GLUTAMATE, ASPARTATE, NITRIC OXIDE

3
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INHIBITORY NEUROTRANSMITTERS ARE?

GLYCINE, GABA, SEROTONIN, DOPAMINE

4
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BOTH ACTS AS AN EXCITATORY AND INHIBITORY NEUROTRANSMITTERS ARE?

ACETYLCHOLINE AND NOREPINEPHRINE

5
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THE RELEASE OF _____ IS BLOCKED BY BOTOX

ACETYLCHOLINE

6
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TRUE OR FALSE. OUR BOTOX IS WORKING ON THE NERVE TERMINAL JUNCTION PART

TRUE

7
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THIS IS A NEUROTOXIN/NEUROMODULATOR AND IS MADE UP OF AMINO ACIDS. IT HAS THE ALPHA AND BETA CHAIN LINKED BY DISULFIDE BOND

BOTULINUM TOXIN

8
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THIS WAS NOT ORIGINALLY FOR TREATING WRINKLES. IT STARTED AS A THERAPEUTIC AGENT USED BY NEUROLOGISTS AND OPHTHALMOLOGIST

BOTOX

9
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THIS IS USED TO TREAT BLEPHAROSPASM AND HEMIFACIAL SPASM DUE TO INVOLUNTARY TWITCHING OF THE EYELID MUSCLES, WHICH IS INJECTED INTO THE MUSCLE

BOTOX

10
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BOTULINUM NEUROTOXINS (BONTS), PRODUCED BY ANAEROBIC BACTERIA _______, ARE THE MOST POTENT NEUROTOXINS

CLOSTRIDIUM BOTULINUM

11
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BONTS ARE CLASSIFIED BY THE CDC AS WHAT CATEGORY?

CATEGORY A BIOTERRORISM AGENT

12
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PROTEINS THAT ARE ONLY MADE OF AA. THEY ARE JUST PEPTIDES AND PROTEINS

SIMPLE PROTEINS

13
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SOLUBLE IN WATER AND DILUTE AQUEOUS SALT SOLUTION; HEAT COAGULABLE

ALBUMIN

14
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INSOLUBLE IN WATER; SOLUBLE IN AQUEOUS SALT SOLUTION; HEAT COAGULABLE

GLOBULIN

15
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SOLUBLE IN DILUTE ACIDS AND ALKALIS; HEAT COAGULABLE

GLUTELIN

16
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ALCOHOL-SOLUBLE PROTEIN

PROLAMINE

17
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LEAST SOLUBLE SIMPLE PROTEIN

ALBUMINOID (SCLEROPROTEIN)

18
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BASIC PROTEIN; SOLUBLE IN WATER, DILUTE ACID AND ALKALI; FOUND IN COMBINATION WITH DNA

HISTONE

19
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SIMPLEST; BASIC; SOLUBLE IN WATER, DILUTE AMMONIA, ACID AND ALKALI; FOUND IN SPERMATOZOA

PROTAMINE

20
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ADDED ANOTHER KIND OF COMPOUND THAT IS LINKED TO THE PROTEIN. MADE UP OF A PROTEIN

CONJUGATED PROTEINS

21
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CONJUGATED PROTEIN WHERIEN THE NUCLEIC ACID IS THE PROSTHETIC GROUP

NUCLEOPROTEINS

22
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COJUGATED PROTEINS THAT CONTAINS CARBOHYDRATES

GLYCOPROTEINS AND PROTEOGLYCANS

23
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WHICH CONJUGATED PROTEINS CONTAINS MORE CARBOHYDRATES?

A. GLYCOPROTEINS

B. PROTEOGLYCANS

B

24
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CONJUGATED PROTEINS WHERE THEY HAVE PHOSPHORIC ACID RESIDUES; HAVE PHOSPHATE GROUP

PHOSPHOPROTEINS

25
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CONJUGATED PROTEINS WHERE IT CONTAINS PROSTHETIC GROUP THAT GIVES COLOR

CHROMOPROTEINS

26
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CONJUGATED PROTEINS ASSOCIATED WITH LIPIDS

LIPOPROTEINS

27
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CONJUGATED PROTEINS THAT CONTAINS MINERALS

METALLOPROTEINS

28
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DERIVED PROTEINS ARE MADE OF DERIVATIVE MATERIALS SUCH AS?

PROTEASOMES AND PEPTONES

29
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TYPE OF PROTEIN THAT IS TOUGH AND IS INVOLVED IN STRUCTURAL FUNCTIONS

FIBROUS PROTEINS

30
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THEY ARE RESPONSIBLE FOR A STRUCTURAL FRAMEWORK IN THOSE CONNECTIVE TISSUES LIKE THE DERMIS

COLLAGEN

31
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COLLAGEN, KERATIN, AND ELASTIN ARE WHAT TYPE OF PROTEINS?

FIBROUS PROTEINS

32
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THIS IS INVOLVED IN MOBILE AND DYNAMIC FUNCTIONS

GLOBULAR PROTEINS

33
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DEHYDROGENASES AND KINASES FUNCTIONS AS?

ENZYMES

34
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FERRITIN AND MYOGLOBIN FUNCTIONS AS?

STORAGE PROTEINS

35
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MYOGLOBIN, DNA BINDING PROTEINS FUNCTIONS AS?

REGULATORY PROTEINS

36
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ELASTIN, RETICULIN, COLLAGEN FUNCTIONS AS?

STRUCTURAL PROTEINS

37
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IMMUNOGLOBULIN, BLOOD CLOTTING FACTORS FUNCTIONS AS?

PROTECTIVE PROTEINS

38
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PLASMA, LIPOPROTEINS FUNCTIONS AS A?

TRANSPORT PROTEINS

39
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ACTIN AND MYOSIN FUNCTION AS A?

CONTRACTILE OR MOTILE PROTEINS

40
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THESE ARE AMINO ACID POLYMERS HAVING, LOW MOLECULAR WEIGHT AND TYPICALLY CONSIST OF LESS THAN 50 AMINO ACIDS

PEPTIDES

41
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SHORTER VERSION OF LARGE PROTEINS

PEPTIDES

42
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MORE THAN 50 AMINO ACIDS

A. PROTEINS

B. OLIGOPEPTIDES

C. POLYPEPTIDES

A

43
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CONSISTING OF 2 TO 10 AMINO ACIDS

A. PROTEINS

B. OLIGOPEPTIDES

C. POLYPEPTIDES

B

44
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HAVE MORE THAN 10 AMINO ACID RESIDUES

A. PROTEINS

B. OLIGOPEPTIDES

C. POLYPEPTIDES

C

45
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CHAINS OF AMINO ACID RESIDUES ARE LINKED BY A?

PEPTIDE BOND

46
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GAMMA-GLUTAMYL-L-’CYSTEINYGLYCINE

GLUTATHIONE

47
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HOW MANY AMINO ACIDS DOES GLUTATHIONE CONTAINS?

3 AMINO ACIDS (TRIPEPTIDE)

48
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PART OF GLUTATHIONE THAT IS SULFUR-CONTAINING AMINO ACID AND CAUSES WHITENING OF MELANOCYTES

CYSTEINE

49
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SUPPLEMENT THAT IS ALSO A SULFUR-CONTAINING AMINO ACID WHICH IS RELATED WITH CYSTEINE

METHIONINE

50
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THIS IS A REDUCING AGENT, DUE TO -SH GROUP

GLUTATHIONE

51
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THIS PROTECTS THE CELL FROM THE DESTRUCTIVE EFFECTS OF OXIDATION BY PEROXIDES

GLUTATHIONE

52
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THIS WORKS IN HAND WITH GLUTATHIONE PEROXIDASE

GLUTATHIONE

53
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THIS IS NON-ESSENTIAL AS IT CAN BE PRODUCED INSIDE THE BODY (LIVER) BUT IT DECREASES IN SYNTHESIS AS WE AGE DUE TO INCREASED CATABOLISM

GLUTATHIONE

54
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GLUTATHIONE ARE ADMINISTERED VIA?

ORAL OR INJECTIBLES

55
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HOW MANY AMINO ACIDS DOES OXYTOCIN AND VASOPRESSIN HAVE?

9 AMINO ACIDS (NANO AMINO ACIDS)

56
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THIS IS INVOLVED IN CHILDBIRTH BY STIMULATING THE CONTRACTIONS OF THE UTERINE WALL/MUSCLE (INFUSED WITH THE IV FLUID)

OXYTOCIN

57
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THIS IS AN ANTIDIURETIC HORMONE (ADH) WHICH STIMULATES WATER REABSORPTION IN KIDNEYS

VASOPRESSIN

58
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A PENTAPEPTIDE (5 AMINO ACIDS); ALSO OPIOID PEPTIDES

MET-ENKEPHALIN AND LEU-ENKEPHALIN

59
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THIS HELPS IN RELIEVING PAIN; IT BINDS TO THE RECEPTORS IN THE BRAIN AND INDUCES ANALGESIA

MET-ENKEPHALIN AND LEU-ENKEPHALIN

60
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PROTEINS WITH 28 AMINO ACID RESIDUES

ATRIAL NATRIURETIC FACTOR (ANF)

61
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THIS STIMULATES THE PRODUCTION OF A DILUTE URINE

ATRIAL NATRIURETIC FACTOR (ANF)

62
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THIS IS THE OPPOSITE OF ENKEPHALIN; THIS STIMULATES THE PERCEPTION OF PAIN

SUBSTANCE P AND BRADYKININ

63
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THIS HAS 29 AMINO ACIDS; OPPOSES THE ACTION OF INSULIN (ANTI-INSULIN)

GLUCAGON

64
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THIS IS AN ARTIFICIAL SWEETENER AND IS PRESENT IN SOFTDRINKS

ASPARTAME

65
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FORMATION OF THE PEPTIDE BOND IS THROUGH THE INTERACTION BETWEEN THE?

ALPHA-CARBOXYL GROUP (1ST) AND ALPHA-AMINO GROUP (2ND)

66
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THIS IS A PARTIAL DOUBLE BOND - SINGLE BOND BUT ACTS AS A DOUBLE BOND; HAS A RIGID STRUCTURE

PLANAR PEPTIDE BOND

67
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THIS IS WHEN THE SIDE CHAINS ARE SITUATED ON OPPOSITE SIDES

COPLANAR

68
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POLAR BUT UNCHARGED; TRANS CONFIGURATION

PLANAR PEPTIDE BOND

69
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ORGANIZATION OF PROTEINS: SEQUENCE OF AMINO ACIDS

PRIMARY STRUCTURE

70
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ORGANIZATION OF PROTEINS: ALPHA HELIX OR BETA SHEET

SECONDARY STRUCTURE

71
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ORGANIZATION OF PROTEINS: 3D SHAPE

TERTIARY STRUCTURE

72
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ORGANIZATION OF PROTEINS: MULTIPLE POLYPEPTIDES

QUATERNARY STRUCTURE

73
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THIS IS THE BACKBONE OF YOUR PROTEIN

PRIMARY STRUCTURE

74
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LINEAR SEQUENCES OF YOUR AMINO ACID RESIDUES

PRIMARY STRUCTURE

75
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IT’S LIKE A STRAIGHT CHAIN OF AMINO ACID RESIDUES

PRIMARY STRUCTURE

76
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QUANTITATIVE AMINO ACID COMPOSITION; SEQUENCE OF AMINO ACIDS; NUMBER OF PEPTIDE CHAIN

PRIMARY STRUCTURE

77
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REFERS TO THE ATOMS THAT PARTICIPATE IN THE FORMATION OF PEPTIDE BONDS

BACKBONE OF A PROTEIN

78
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THE SIGNIFICANT BOND IN PRIMARY STRUCTURE IS CALLED THE?

PEPTIDE BOND/AMIDE BOND

79
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REFERS TO THE COILING OR A FORMATION OF A DIFFERENT FORM OF YOUR PRIMARY STRUCTURE

SECONDARY STRUCTURE

80
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THIS HAPPENS DUE TO THE FORMATION OF HYDROGEN BONDS BETWEEN PEPTIDE BONDS

SECONDARY STRUCTURE

81
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TWO TYPES OF SECONDARY STRUCTURE ARE THE?

COILS OR HELICES AND SHEETS OR PLEATS

82
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INTRACHAIN HYDROGEN BONDING

A. COILS OR HELICES

B. SHEETS AND PLEATS

A

83
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INTERCHAIN HYDROGEN BONDING

A. COILS OR HELICES

B. SHEETS AND PLEATS

B

84
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THIS WAS DISCOVERED BY LINUS PAULING IN 1951

ALPHA HELIX

85
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STABILIZED BY INTER-RESIDUE HYDROGEN BONDS FORMED BETWEEN THE H ATOM ATTACHED TO A PEPTIDE N AND THE CARBONYL O ATOM

ALPHA HELIX

86
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IN ____, EACH PEPTIDE BOND PARTICIPATES IN HYDROGEN BONDING

ALPHA HELIX

87
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THIS FORMS SPONTANEOUSLY AS IT IS THE LOWEST ENERGY, MOST STABLE CONFORMATION FOR A POLYPEPTIDE CHAIN

ALPHA HELIX

88
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IN ALPHA HELIX, ______ EXTEND OUTWARD FROM THE HELIX

AMINO ACID R GROUPS

89
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TRUE OR FALSE. PRESENCE OF ADJACENT SIMILARLY CHARGED AMINO ACIDS DESTABILIZE THE ALPHA HELIX

TRUE

90
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TRUE OR FALSE. PRESENCE OF ADJACENT BULKY R GROUPS CAN DESTABILIZE ALPHA HELIX

TRUE

91
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TRUE OR FALSE. PRESENCE OF YOUR PROLINE CAN BREAK YOU ALPHA HELICAL STRUCTURE AS IT CONTAINS RIGID RING THAT PREVENTS THE N-C BOND FROM ROTATING

TRUE

92
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THIS IS THE SECOND MOST COMMONLY OCCURRING PROTEIN SECONDARY STRUCTURE

BETA-PLEATED SHEET

93
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THIS IS FORMED WHEN 2 OR MORE ALMOST FULLY EXTENDED POLYPEPTIDE CHAIN LIE SIDE BY SIDE SUCH THAT HYDROGEN BONDING OCCURS BETWEEN ADJACENT PEPTIDE CHAINS

BETA-PLEATED SHEET

94
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TRUE OR FALSE. THERE IS ALSO A BETA-PLEATED SHEET THAT HAS ONLY 1 POLYPEPTIDE, IT WILL JUST BEND ON ITS OWN

TRUE

95
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THIS LIE ABOVE OR BELOW THE ZIGZAGGING PLANES OF THE PLEATED SHEET AND ARE NEARLY PERPENDICULAR TO THEM

R GROUPS

96
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THESE HAVE SHARP/SOFT BENDS

BETA-PLEATED SHEET

97
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AMINO ACIDS WITH LESS BULKY R GROUPS ARE PRESENT IN?

BETA-PLEATED SHEET

98
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DIFFERENT ARRANGEMENT OF BETA-SHEETS WHEREIN NEIGHBORING H BONDED POLYPEPTIDE CHAINS RUN IN OPPOSITE DIRECTION; MORE STABLE AND ARE MORE COMMON

ANTI-PARALLEL BETA-SHEET

99
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DIFFERENT ARRANGEMENT OF BETA-SHEETS WHEREIN HYDROGEN BONDED CHAINS EXTEND IN THE SAME DIRECTION

PARALLEL BETA SHEET

100
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FACTORS THAT DESTABILIZE BETA-PLEATED SHEET ARE?

BULKY R GROUPS AND R GROUPS WITH LIKE CHARGES