Professor Too Bright

8/19/2019 Professor Too Bright

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PROFE S SOR TOO

BRIGHMD SC 100 1 PBL PROB

T U TOR: DR S.


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LIST OF OBJECTIVES

1. DISCUSS THE HISTOLOGY OF HUMAN RED BLOOD CELLS. BRIEFLY COMPARE THE HISTOLOGY OF HUMAN CHICRED BLOOD CELLS

2. COMPARE THE AMINO ACIDS NEEDS OF HUMANS AND SOME DOMESTIC ANIMALS3. EXPLAIN HAT IS MEANT BY THE TERMS PRIMARY SECONDARY TERTIARY AND !UATERNARY STRUCTURE O". BRIEFLY DISCUSS HO THE PROPERTIES OF AMINO ACIDS AFFECT THE PRIMARY SECONDARY TERTIARY AN

!UATERNARY STRUCTURE OF PROTEINS

#. EXPLAIN THE BASIS OF SICKLE CELL ANAEMIA $. DESCRIBE THE DIFFERENT TYPES OF POINT MUTATIONS AND THEIR POSSIBLE EFFECTS ON PROTEIN STRUCTFUNCTION

%. DISCUSS THE ROLE OF EPIDEMIOLOGY IN UNDERSTANDING CAUSES OF ILL HEALTH AND THE SPREAD OF DISE


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DISCUSS THE HISTOLOGY OF HUMAN RED BLOOD CELLS AND BRIEFLYCOMPARE THE HISTOLOGY OF HUMAN CHICKEN AND RAT RED BLOOD

• FIRSTLY& HISTOLOGY IS A GREEK ORD HICH TRANSLATES TO HISTOS 'TISSUE'& AND LOGIAHENCE HISTOLOGY IS MICROSCOPIC ANATOMY.

• IN COMPARING THE HISTOLOGY AMONG HUMANS& RATS AND CHICKEN BLOOD CELLS E MUSTAKE INTO ACCOUNT THAT BOTH RATS AND HUMANS ARE MAMMALS& HILE& CHICKENS ARE N

THEREFORE SIGNIFIES THAT THERE ILL BE SOME SIGNIFICANT DIFFERENCES BETEEN THES

HISTOLOGY.


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DISCUSS THE HISTOLOGY OF HUMAN RED BLOOD CEL AND BRIEFLY COMPARE THE HISTOLOGY OF HUMANCHICKEN AND RAT RED BLOOD CELLS


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DISCUSS THE HISTOLOGY OF HUMAN RED BLOOD CELLS AND BRIEFLY COMPARE THE HIOF HUMAN CHICKEN AND RAT RED BLOOD CELLS

• HUMAN ERYTHROCYTES UNDERGO THEIR MATURATION IN THE BONE MARRO& HICH CONSSEVERAL STAGES IN HICH ALL NUCLEIC MATERIAL IS REMOVED FROM THE CELLS& AND THE P

HAEMOGLOBIN IS MASS SYNTHESI*ED ITHIN THE CELLS. EVENTUALLY AROUND +0, OF THE

EIGHT OF THE CELL IS MADE UP OF THIS PROTEIN. THE NUCLEUS IS LOST FROM THE CELL. TH

BLOOD CELLS CAN THEN ENTER THE CIRCULATION. THE CELL ASSUMES A BI-CONCAVE SHAPE

CHARACTERISTIC OF HUMAN RED BLOOD CELLS.


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DISCUSS THE HISTOLOGY OF HUMAN RED BLOOD CELLS ANDBRIEFLY COMPARE THE HISTOLOGY OF HUMAN CHICKEN ANRED BLOOD CELLS

Human RBC viewed under light microscope


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DISCUSS THE HISTOLOGY OF HUMAN RED BLOOD CEL AND BRIEFLY COMPARE THE HISTOLOGY OF HUMANCHICKEN AND RAT RED BLOOD CELLS

• HUMAN ERYTHROCYTES ARE BICONCAVE DISC SHAPED ITH OUT A NUCLEUS.

• IT IS A GENETIC ADAPTATION ITHOUT NUCLEUS MORE SPACE FOR HAEMOGLOBIN IS FREE. AHAEMOGLOBIN IS THE CARRIER OF OXYGEN. HENCE& THIS CAN SIMPLY BE EXPLAINED BY THE N

MAXIMUM SURFACE AREA FOR MAXIMUM OXYGEN CARRYING CAPACITY.


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DISCUSS THE HISTOLOGY OF HUMAN RED BLOOD CELLS AND BRIEFLYCOMPARE THE HISTOLOGY OF HUMAN CHICKEN AND RAT RED BLOOD

•THE RBC OF CHICKENS HOEVER& IS LARGE& CONVEX& ITH AN OVAL NUCLEUS. THEY ALSO CO

THREE FILAMENT SYSTEMS THAT ARE FOUND IN THE MAJORITY OF SOMATIC CELLS INTERME

FILAMENTS& MICROTUBULES AND ACTIN FILAMENTS/ HEREAS HUMAN RBC ONLY CONTAIN

FILAMENT SYSTEM ACTIN FILAMENTS/. OTHER THAN THAT& THE HAEMOGLOBIN OF CHICKEN B

IS LARGELY SIMILAR TO HUMAN RED BLOOD CELLS& ONLY DIFFERING BY TO AMINO ACIDS IN

PRIMARY SE!UENCE.


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DISCUSS THE HISTOLOGY OF HUMAN RED BLOOD CELLS AND BRIEFLY COMPAREHISTOLOGY OF HUMAN CHICKEN AND RAT RED BLOOD CELLS

•Chicken erythrocytes are elongated and nucleated:


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DISCUSS THE HISTOLOGY OF HUMAN RED BLOOD CELLS AND BRIEFLY COMPARE HISTOLOGY OF HUMAN CHICKEN AND RAT RED BLOOD CELLS

Chicken RBC under light microscope


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COMPARE THE AMINO ACIDS NEEDS OF HUMANS AND SOME DOMESTIC A

• AMINO ACIDS ARE A GROUP OF COMPOUNDS ITH AT LEAST 1 AMINO GROUP& A CARBOXYL GROUP AND A DISTINC

• EIGHT AMINO ACIDS ARE ESSENTIAL FOR HUMANS& AS THE BODY CANNOT PRODUCE THEM BY THEMSELVES& AND TSUPPLIED EXTERNALLY. THESE ARE: ISOLEUCINE& LEUCINE& LYSINE& METHIONINE& PHENYLALANINE& THREONINE& TRYP

VALINE.

• ARGININE AND HISTIDINE FORM THE GROUP OF SO-CALLED SEMI-ESSENTIAL AMINO ACIDS. THEY HAVE TO BE CONSDIET UNDER CERTAIN CIRCUMSTANCES.

• THE TEN NON-ESSENTIAL AMINO ACIDS ARE ABLE TO BE PRODUCED IN THE BODY. THE FOLLOING AMINO ACIDS FACATEGORY: ALANINE& ASPARAGINE& ASPARTIC ACID& CYSTEINE& GLUTAMINE& GLUTAMIC ACID& GLYCINE& PROLINE& SE

TYROSINE.


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EXPLAIN HAT IS MEANT BY THE TERMS PRIMARY SECONTERTIARY AND !UATERNARY STRUCTURE OF PROTEINS

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EXPLAIN HAT IS MEANT BY THE TERMS PRIMARYSECONDARY TERTIARY AND !UATERNARY STRUCTURPROTEINS


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• THE THREE-DIMENSIONAL STRUCTURE OF THE ENTIRE POLYPEPTIDE CHAIN IS THE TERTIARYSTRUCTURE OF A PROTEIN.

• THE TERTIARY STRUCTURE OF A PROTEIN IS HELD TOGETHER BY FOUR DIFFERENT TYPES OF BINTERACTIONS

•DISULPHIDE BONDS& IONIC BONDS& HYDROGEN BONDS& HYDROPHOBIC AND HYDROPHILIC

INTERACTIONS.


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• SOME PROTEINS ARE MADE UP OF MULTIPLE POLYPEPTIDE CHAINS SOMETIMES ITH AN INOCOMPONENT CALLED A PROSTHETIC GROUP FOR EXAMPLE& A HAEM GROUP IN HEMOGLOBIN

POLYPEPTIDE INCLUDING THE PROSTHETIC GROUP IS REFERRED TO AS A SUBUNIT OF THE PR

SAME FORCES AND BONDS THAT CREATE TERTIARY STRUCTURES ALSO HOLD THESE STRUCT

TOGETHER IN A STABLE COMPLEX KNO AS THE !UATERNARY STRUCTURE OF THE PROTEIN

• THESE PROTEINS THAT FORM !UATERNARY STRUCTURES ARE ONLY ABLE TO FUNCTION IF ALL ARE PRESENT THE POLYPEPTIDE CHAIN AND PROSTHETIC GROUP/.


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BRIEFLY DISCUSS HO THE PROPERTIES OF AMINO ACIDS AFFECT THE PRIMARY SECONDTERTIARY AND !UATERNARY STRUCTURE OF PROTEINS

• IN THE PRIMARY STRUCTURE& AMINO ACIDS& AS THEIR NAME INDICATES& CONTAIN BOTH A BASIC AMINO GROUP AN

CARBOXYL GROUP. THIS DI FUNCTIONALITY ALLOS THE INDIVIDUAL AMINO ACIDS TO JOIN TOGETHER IN LONG CHAFORMING PEPTIDE BONDS: AMIDE BONDS BETEEN THE -NH2 OF ONE AMINO ACID AND THE -COOH OF ANOTHER.

• TO MAIN TYPES OF SECONDARY STRUCTURE ARE THE ALPHA HELIX AND THE BETA STRAND . ITH THE ALPHAMOST IMPORTANT IS THAT THE N-H GROUP OF AN AMINO ACID FORMS A HYDROGEN BOND ITH THE CO GROUP OF

ACID FOUR RESIDUES EARLIER THIS REPEATED HYDROGEN BONDING IS THE MOST PROMINENT CHARACTERISTIC O

DIFFERENT AMINO-ACID SE!UENCES HAVE DIFFERENT PROPENSITIES FOR FORMING -HELICAL STRUCTURE. METHIO

LEUCINE& UNCHARGED GLUTAMATE& AND LYSINE ALL HAVE ESPECIALLY HIGH HELIX-FORMING PROPENSITIES& HEREA

GLYCINE HAVE POOR HELIX-FORMING PROPENSITIES.

• ITH THE BETA STRAND &IT IS A STRETCH OF POLYPEPTIDE CHAIN TYPICALLY 3 TO 10 AMINO ACIDS LONG ITH B ALMOST FULLY EXTENDED CONFORMATION. TO ANTIPARALLEL STRANDS ARE LINKED BY A SHORT LOOP OF TO TOOF HICH ONE IS FRE!UENTLY A GLYCINE OR A PROLINE& BOTH OF HICH CAN ASSUME THE UNUSUAL DIHEDRAL-AN

CONFORMATIONS RE!UIRED FOR A TIGHT TURN. HOEVER& INDIVIDUAL STRANDS CAN ALSO BE LINKED IN MORE EL

ITH LONG LOOPS THAT MAY CONTAIN ALPHA HELICES OR EVEN ENTIRE PROTEIN DOMAINS

• IN THE TERTIARY STRUCTURE THE THREE-DIMENSIONAL SHAPE OF A PROTEIN MAY SEEM IRREGULAR AND RANDOM

https://en.wikibooks.org/w/index.php?title=Alpha_helix&action=edit&redlink=1https://en.wikibooks.org/w/index.php?title=Beta_strand&action=edit&redlink=1https://en.wikibooks.org/w/index.php?title=Glycine&action=edit&redlink=1https://en.wikibooks.org/w/index.php?title=Proline&action=edit&redlink=1https://en.wikibooks.org/w/index.php?title=Turn_(biochemistry)&action=edit&redlink=1https://en.wikibooks.org/w/index.php?title=Alpha_helix&action=edit&redlink=1https://en.wikibooks.org/w/index.php?title=Alpha_helix&action=edit&redlink=1https://en.wikibooks.org/w/index.php?title=Turn_(biochemistry)&action=edit&redlink=1https://en.wikibooks.org/w/index.php?title=Proline&action=edit&redlink=1https://en.wikibooks.org/w/index.php?title=Glycine&action=edit&redlink=1https://en.wikibooks.org/w/index.php?title=Beta_strand&action=edit&redlink=1https://en.wikibooks.org/w/index.php?title=Alpha_helix&action=edit&redlink=1


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BRIEFLY DISCUSS HO THE PROPERTIES OF AMINO ACIDS AFFECT THE PRIMARY SECONDARY TERTIA!UATERNARY STRUCTURE OF PROTEINS

• PHENYLALANINE OR ISOLEUCINE TEND TO BE BURIED ON THE INTERIOR OF THE PROTEIN MOLECULE THESHIELDING THEM FROM THE A!UEOUS MEDIUM. THE ALKYL GROUPS OF ALANINE& VALINE& LEUCINE AND

OFTEN FORM HYDROPHOBIC INTERACTIONS BETEEN ONE-ANOTHER& HILE AROMATIC GROUPS SUCOF PHENYLALANINE AND TYROSINE OFTEN STACK TOGETHER. ACIDIC OR BASIC AMINO ACID SIDE-CHA

GENERALLY BE EXPOSED ON THE SURFACE OF THE PROTEIN AS THEY ARE HYDROPHILIC.

• THE FORMATION OF DISULPHIDE BRIDGES BY OXIDATION OF THE SULFHYDRYL GROUPS ON CYSTEINE ISIMPORTANT ASPECT OF THE STABILI*ATION OF PROTEIN TERTIARY STRUCTURE& ALLOING DIFFERENT

PROTEIN CHAIN TO BE HELD TOGETHER COVALENTLY. ADDITIONALLY& HYDROGEN BONDS MAY FORM BET

DIFFERENT SIDE-CHAIN GROUPS. AS ITH DISULPHIDE& THESE HYDROGEN BONDS CAN BRING TOGETH

PARTS OF A CHAIN THAT ARE SOME DISTANCE AAY IN TERMS OF SE!UENCE. SALT BRIDGES & IONIC INTBETEEN POSITIVELY AND NEGATIVELY CHARGED SITES ON AMINO ACID SIDE CHAINS& ALSO HELP TO S

TERTIARY STRUCTURE OF A PROTEIN.

• LASTLY IN THE !UATERNARY STRUCTURE THE FINAL SHAPE OF THE PROTEIN COMPLEX IS ONCE AGASTABILI*ED BY VARIOUS INTERACTIONS& INCLUDING HYDROGEN-BONDING& DISULFIDE-BRIDGES AND S


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EXPLAIN THE BASIS OF SICKLE CELL ANAEMIA

• THIS DISEASE IS DUE TO A POINT MUTATION ON CHROMOSOME 11. THE $TH AMINO ACID ON THCHAIN IN NORMAL HAEMOGLOBIN IS GLUTAMIC ACID HICH IS HYDROPHILIC. IT IS CODED F

ON THE NORMAL DNA. DUE TO A BASE SUBSTITUTION THAT OCCURS IN THE SECOND POSITIO

TRIPLET& IT CHANGES TO CAC ON THE MUTANT DNA AND GUG ON THE MUTANT RNA. THIS COD

AMINO ACID VALINE HICH IS HYDROPHOBIC. THIS ILL RESULT IN THE HAEMOGLOBIN CRY

INTO ROD LIKE FIBRES AS IT IS LESS SOLUBLE THAN NORMAL HAEMOGLOBIN FORMING SICKL

HAEMOGLOBIN.


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EXPLAIN THE BASIS OF SICKLE CELL ANAEMIA

• EFFECT

• SICKLED SHAPE OF HAEMOGLOBIN CAUSES THE TRANSPORT OF LESS OXYGEN SO THE PERSON IS SHORT AND EXPERIENCES FATIGUE.

• THE ABNORMAL CELLS CLUMPS TOGETHER AND CAUSES THE ABNORMAL FLO OF BLOOD.

• ISSUE

• HO IS POINT MUTATION RELATED TO SICKLE CELL ANAEMIA

• A POINT MUTATION AFFECTS A SINGLE BASE EITHER FIRST& SECOND OR THIRD POSITION/ ON THE DNA. TCAN AFFECT THE FOLDING OF THE POLYPEPTIDE CHAIN& ITS SHAPE AND PROPERTIES. THERE ARE DIFFERE

POINT MUTATIONS AND A BASE SUBSTITUTION HICH OCCURS IN SICKLE CELL ANAEMIA IS ONE OF THE

• REFERENCE : MRS.CAROLYN BALLY-GOSINE BIOLOGY CLASSES/

DESCRIBE THE DIFFERENT TYPES OF POINT MUTATION


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DESCRIBE THE DIFFERENT TYPES OF POINT MUTATIONTHEIR POSSIBLE EFFECTS ON PROTEIN STRUCTURE AFUNCTION

• A POINT MUTATION IS AN ALTERATION IN THE SE!UENCE OF DNA DEOXYRIBONUCLEIC ACID/ RESULTING FRONUCLEOTIDE BASE CHANGE SUBSTITUTION/& INSERTION OR DELETION& USUALLY OCCURRING DURING DNA

• THESE MUTATIONS CAN BE SPONTANEOUS OR INDUCED BY MUTAGENS & HICH ARE PHYSICAL OR CHEMICAHICH CHANGE THE NUCLEOTIDE SE!UENCE OF DNA. SOME EXAMPLES OF MUTAGENS ARE IONISING RADIAT

CARCINOGENIC CHEMICALS.

• LONG CHAINS OF NUCLEOTIDES MAKE UP DNA HICH IS STORED IN THE NUCLEUS HOEVER PROTEINS ARE

IN THE CYTOPLASM AT THE RIBOSOMES. IN ORDER FOR THE MESSAGE CODED ON A GENE& A SECTION OF DNATRANSCRIPTION INTO MRNA MUST OCCUR. TO MAKE THIS MRNA& THE GENE IS READ THREE BASES AT A TIM

CALLED TRIPLETS. EACH TRIPLET ON DNA AND THE CORRESPONDING CODON ON MRNA CODE FOR A SPECIFI

POINT MUTATIONS RESULT IN AN ALTERED AY THAT THE DNA IS READ LEADING TO A POTENTIAL DIFFERENT

FOR HICH IT CODES AND THEREFORE A POSSIBLE CHANGE IN THE PROTEIN. THIS COULD HAVE NEGATIVE O

EFFECTS ON THE STRUCTURE AND FUNCTION OF THE PARTICULAR CHANGED PROTEIN.


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DESCRIBE THE DIFFERENT TYPES OF POINT MUTATIONS AND THEIR PEFFECTS ON PROTEIN STRUCTURE AND FUNCTION

• THERE ARE TO SYSTEMS HICH ARE USED TO CATEGORISE POINT MUTATIONS. IN THE FIRST SYSTEMUTATION IS CATEGORISED AS A TRANSITION IF A PURINE BASE IS REPLACED ITH ANOTHER PURIN

PYRIMIDINE IS REPLACED ITH ANOTHER PYRIMIDINE BASE. TRANSVERSIONS ARE REPLACEMENTS O

TYPE E.G. A PURINE/ ITH THE OTHER A PYRIMIDINE IN THIS CASE/.

• IN THE FUNCTIONAL CATEGORISATION OF POINT MUTATIONS& THE MUTATION IS CHARACTERISED BY THAS ON THE AMINO ACID SE!UENCE OF THE PROTEIN. THE DIFFERENT CATEGORIES FOLLO:

• FREESE& E. 1+#+/. THE DIFFERENCE BETEEN SPONTANEOUS AND BASE-ANALOGUE INDUCED MUTATIPHAGE T". PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERI

$22$33.


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EXPLAIN THE BASIS OF SICKLE CELL ANAEMIA • BASE- AIR SUBSTITION• NONSENSE MUTATION: A CODON FOR AN AMINO ACID IS REPLACED BY A TERMINATION CODON& THUS INTERRUP

TRANSLATION PROCESS AT THAT POINT IN THE PROTEIN CHAIN. A SHORTER PROTEIN RESULTS.

• SILENT MUTATION : BECAUSE EACH AMINO ACID CAN BE CODED FOR BY MORE THAN NUCLEOTIDE SE!UENCE $"REPRESENT 20 AMINO ACIDS IN TOTAL/ A CHANGE IN NUCLEOTIDE CAN RESULT IN A NE CODON THAT CODES FO

AMINO ACID. THE RESULTING PROTEIN IS IDENTICAL TO THE NORMAL PROTEIN HENCE IT OULD HAVE THE SAME

STRUCTURE OF THE ORIGINAL PROTEIN.

• MISSENSE MUTATION : A CODON FOR AN AMINO ACID IS REPLACED BY ONE FOR A DIFFERENT AMINO ACID. IN THDIFFERENT PROTEIN IS CREATED. THIS CATEGORY IS FURTHER SPLIT BASED ON THE EFFECT THE RESULTING PROT

THE ORGANISM:

• IN CONSERVATIVE MUTATIONS THE PROPERTIES OF THE AMINO ACID AND THUS THE PROTEIN ARE SIMILAR TO THOSE OFTHE !UATERNARY STRUCTURE OF THE PROTEIN IS SIMILAR ENOUGH TO HAVE THE SAME EFFECT AS THE ORIGINAL. AS A R

FUNCTIONING OF THE PROTEIN AND THE ORGANISM ARE NOT SIGNIFICANTLY CHANGED.

• IN NON-CONSERVATIVE MUTATIONS THE SUBSTITUTED AMINO ACID HAS DIFFERENT PROPERTIES THAN THE ORIGINAL& CPROTEIN TO LOSE OR CHANGE ITS FUNCTION. THIS FRE!UENTLY RESULTS IN DISEASE AS THE !UATERNARY STRUCTURE

EXAMPLE& IN SICKLE-CELL DISEASE


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DESCRIBE THE DIFFERENT TYPES OF POINT MUTATIONS AND THEIR POSSIBLE EFFECTS ON PROTSTRUCTURE AND FUNCTION

• BASE- AIR INSERTIONS OR DELETIONS .FRAMESHIFT MUTATIONS/• DELETION: INVOLVES THE LOSS OF ONE BASE PAIR FROM THE DNA MOLECULE. AS THE BASES

AS TRIPLETS& IF ONE PAIR GOES MISSING& THE HOLE SE!UENCE OULD BE READ DIFFERENT

IS CALLED A FRAME SHIFT.

• INSERTION: INVOLVES THE ADDITION OF A NE PAIR OF BASES INTO THE DNA. IT IS SIMILARDELETION AS IT OULD ALAYS CAUSE A FRAME SHIFT. THIS OULD RESULT IN A SERIOUS E

THE PROTEIN HICH IS MADE.

• EACH MUTATION LISTED ABOVE APART FROM SILENT MUTATION CAN PRODUCE A DIFFERENT A

SE!UENCE PRIMARY STRUCTURE/ IN THE PROTEIN THAT THE DNA IS CODING FOR. CONSE!USECONDARY AND TERTIARY STRUCTURE OF THE PROTEIN OULD BE DIFFERENT FROM THE OR

PROTEIN. THIS OULD THEN LEAD TO THE PROTEINS STRUCTURE BEING DISRUPTED.

DESCRIBE THE DIFFERENT TYPES OF POINT MUTATIONS AND THEIR P


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DESCRIBE THE DIFFERENT TYPES OF POINT MUTATIONS AND THEIR PEFFECTS ON PROTEIN STRUCTURE AND FUNCTION

FIGURE 1: DIFFERENT TYE! "F "INT #UT$TI"N!


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DISCUSS THE ROLE OF EPIDEMIOLOGY IN UNDERSTANDING CAUSES OF ILL HEALTH AND THE SPDISEASE

• DEFINITION: EPIDEMIOLOGY IS THE STUDY OF THE ORIGIN AND CAUSES OF DISEASES IN A COMMUNITYSCIENTIFIC METHOD OF INVESTIGATION PROBLEMSOLVING USED BY DISEASE DETECTIVES EPIDEMIOL

LABORATORY SCIENTISTS& STATISTICIANS& PHYSICIANS AND OTHER HEALTH CARE PROVIDERS& AND PU

PROFESSIONALS TO GET TO THE ROOT OF HEALTH PROBLEMS AND OUTBREAKS IN A COMMUNITY. HY

STUDY OUTBREAKSP :

• OUTBREAKS ARE IMPORTANT PUBLIC HEALTH EVENTS AND MAY REPRESENT BREAKDONS IN PUBLIC HMEASURES AND ALLOS PREVENTATIVE MEASURES TO BE PUT IN PLACE TO PREVENT FUTURE OUTBREA

SAMESIMILAR DISEASES.

• OUTBREAKS ARE EXPERIMENTS OF NATURE AND PROVIDE AN OPPORTUNITY TO LEARN MORE ABOUT THHISTORY OF INFECTIOUS DISEASES.

DISCUSS THE ROLE OF EPIDEMIOLOGY IN UNDERSTANDING OF ILL HEALTH AND THE SPREAD OF DISEASE


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OF ILL HEALTH AND THE SPREAD OF DISEASE

• STE S IN AN OUTBREAK INVESTIGATION :

• VERIFY THE DIAGNOSIS - THIS IS IMPORTANT TO RULE OUT MISDIAGNOSIS AND LABORATORY ERROCERTAIN ITQS THE REAL THING& AND NOT A FALSE ALARM. THIS IS ESPECIALLY IMPORTANT IN HOSPITA

BUT IN OTHERS AS ELL.

• CONFIRM THE EXISTENCE OF AN OUTBREAK - THIS STEP RE!UIRES YOU TO COMPARE THE MAGNIPRESENT PROBLEM ITH SOME TYPE OF BASELINE. TO DO THIS& YOU NEED TO FIRST ESTABLISH A BAS

NEED TO CONSIDER& FOR EXAMPLE& HETHER IT SHOULD BE THE PERIOD IMMEDIATELY PRECEDING TH

PROBLEM& OR THE CORRESPONDING PERIOD FROM THE PREVIOUS YEAR.

• IDENTIFY AND COUNT CASES - FOR THIS STEP YOU MUST FIRST ESTABLISH A CASE DEFINITION. A CDEFINITION IS A STATEMENT HICH SPECIFIES A PERSON ITH SOME SET OF SYMPTOMS ANDOR SI

LABORATORY DIAGNOSIS HICH OCCURRED DURING SOME TIME PERIOD USUALLY DEFINED AS THE O

PERIOD. BASED ON THE CRITERIA IN THE CASE DEFINITION PERSONS SHOING ONLY THESE ILL BE I

BEING EXPOSED TO THE OUT BREAK AND ILL BE COUNTED AS A CASE. ALL DATA IS COLLECTED DURIN

DISCUSS THE ROLE OF EPIDEMIOLOGY IN UNDERSTANDING CAUSES OF ILL HEALTH AND TH


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DISCUSS THE ROLE OF EPIDEMIOLOGY IN UNDERSTANDING CAUSES OF ILL HEALTH AND THOF DISEASE

• ORIENT DATA IN TERMS OF TIME& LAC E AND ERSON - THE FIRST STEP IN ORIENTING THUSUALLY TO CONSTRUCT A LINE LISTING. IN A LINE LIST EACH COLUMN REPRESENTS AN IMPO

VARIABLE& SUCH AS NAME& AGE& SEX& CASE CLASSIFICATION AND SO ON HILE EACH RO REDIFFERENT CASE. THE LINE LIST CAN BE HAND-RITTEN OR COMPUTER GENERATED. FOLLO

LINE LIST AND DATA COLLECTED IS USED TO CLASSIFY THE DATA IN TERMS OF TIME EPIDEMIC

PLACE SPOT MAPS/ AND PERSON COMPARE GROUPS/.

• FORMULATE AND TEST HY OTHESIS IN MOST INVESTIGATIONS THE TIME& PLACE& AND PORIENTATION PROVIDES ENOUGH INFORMATION TO DETERMINE HO AND HY THE EPIDEMI

HOEVER SOME CASES RE!UIRE FURTHER INVESTIGATION. HYPOTHESES& BASED ON AVAILA

ILL BE GENERATED TO EXPLAIN THE OUTBREAK IN ORDER TO DETERMINE TYPE OF EXPOSURE

SOURCE OR RESERVOIR& MODE OF TRANSMISSION& OR RISK FACTORS.

DISCUSS THE ROLE OF EPIDEMIOLOGY IN UNDERSTANDING CAUSES OF ILL HEALTH AND THE SP


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DISCUSS THE ROLE OF EPIDEMIOLOGY IN UNDERSTANDING CAUSES OF ILL HEALTH AND THE SPDISEASE

• CONDUCT ANIMAL OR ENVIRONMENTAL STUDIES TO DETERMINE THE SOURCE OF THE AGENT - THE TYSTUDIES INDICATED ILL DEPEND ON THE AGENT AND THE SUSPECTED MODE OF TRANSMISSION. FOR EXAMP

FOODBORNE OUTBREAKS& ADDITIONAL INVESTIGATIONS OFTEN INCLUDE INSPECTION OF THE FOOD PREPARA

IF CONTAMINATION IS SUSPECTED TO HAVE OCCURRED PRIOR TO THE TIME OF FOOD PREPARATION A TRACE

INVESTIGATION MAY BE CONDUCTED.

• IM LEMENT CONTROL AND REVENTION MEASURES - AT THIS POINT MEASURES ARE PUT IN PLACE TO COUTBREAK AND PREVENT ADDITIONAL CASES AND RECURRENCES OF THE PROBLEM. THESE MEASURES INCLU

• 1/ ELIMINATE THE SOURCE OR EXPOSURE OF SUSCEPTIBLE PERSONS TO THE SOURCE OF THE AGENT. E.G. REMSOURCE OF CONTAMINATION& REMOVE PERSONS FROM EXPOSURE& INACTIVATE OR NEUTRALI*E THE AGENT IN

ISOLATE ANDOR TREAT INFECTED PERSONS.

• 2/ INTERRUPT SPREAD FROM THE SOURCE TO SUSCEPTIBLE PERSONS& STERILI*E OR INTERRUPT ENVIRONMESOURCES OF SPREAD ATER& FOOD& AIR/& CONTROL MOS!UITO OR INSECT TRANSMISSION& IMPROVE PERSO

SANITATION ASH HANDS/.

• 3/ PROTECT SUSCEPTIBLE PERSONS E.G. VACCINATION& PROPHYLACTIC CHEMOTHERAPY.

• SOURCE : COURSES.ASHINGTON.EDU*EPI#2$PAPERS0+INVESTIGATIONS

Professor Too Bright

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