View Full Version : Bio Chemistry
- How do you measure the pollution in water
- Where does ATP rank on a scale of phosphate transfer potential? What is the
- What is the major advantage of Edman’s reagent
- What reagents can be used to break disulphide bonds
- Describe the classification of all amino acids
- What are the structures of ATP, ADP, PPi and Pi
- What features do the helix and the sheet have in common
- What are the differences and respective advantages to electrophoresis, SDS PAGE
- What reaction is catalyzed by proteases? What steps are involved in determining the
- What types of changes can be used to effect fractional precipitation of proteins
- What role does pro line play in tertiary structures
- What factors contribute to the enthalpy change when a denatured protein folds up
- How much empty space is found in globular proteins
- Why don’t all proteins have methionine as the N-terminal amino acid
- Why is the t-butyloxy carbonyl protecting group such a good choice for amino acid
- How does H-bonding in the helix differ from that in the sheet
- How flexible are protein structures
- What causes aromatic rings to stick to each other
- What does a sedimentation coefficient measure
- How can proteins be denatured and renatured
- What types of molecules can be purified via affinity chromatography
- What kinds of proteins are involved in facilitating protein folding
- Which properties of water are unusual for its size, and caused by hydrogen bonding
- What type of column is generally used to separate amino acids from each other
- Cells are in non equilibrium, open systems. In what way is thermodynamics useful in
- How are coupled reactions used in biochemistry
- Why is it necessary to cleave proteins with at least two different reagents during
- What are hydrophobicity scales, and how are they used
- What is the difference between pH and pKa
- How do cationic exchange resins differ from anionic exchange resins
- How does a random coil differ from an irregularly structured region
- Why is it usually necessary to cleave proteins into smaller fragments for sequencing
- What types of primary structures destabilize helices
- What are the standard state conditions for biochemical thermodynamics
- What are the structures of the products of this reaction, and how are they identified
- From a thermodynamic perspective, why doesn't hexane dissolve in water
- Where do hydrophobic and hydrophilic residues usually end up after protein folding
- How are free energy, equilibrium and spontaneity related to each other
- Why are free cysteines treated with iodo acetate prior to protein sequencing
- How does a buffer work
- What factors contribute to the entropy change when a denatured protein folds up
- How are free energy changes dependent upon the reaction pathway
- What factors cause the hydrolysis of ATP so exergonic
- What functional group is hydrolyzed in the hydrolysis of ATP to ADP and Pi
- What types of proteins contain disulphide bonds
- What are the structural and stability consequences of electron de localization in
- What role do disulphide bonds play in protein folding, and in protein stability
- How are reaction rates dependent upon free energy changes
- What kinds of compounds are water soluble? Why
- How can peptide bonds be made from amino acids without activating the amino acids
- Why are right-handed helices more stable than left-handed helices
- What are the various types of non covalent attractive forces
- What types of molecules form bi layers
- How are free energy changes related to enthalpy changes and entropy changes
- How can one use the pH and the pKa to determine the acid-base form of a compound
- What types of things happen to proteins during post translational processing
- How does molecular exclusion chromatography work
- What factors cause salting in and salting out of macromolecules
- Why does ion-exchange chromatography generally use a salt gradient or a pH gradient
- What is meant by “cooperative folding” of proteins
- How does hplc differ from normal column chromatography, and what are its advantages
- How does the stability of peptides compare with that of amino acids
- What factors can change the pKa value of an amino acid residue, and in which
- How is the actual free energy change for a process related to the standard free
- What role does the primary structure play in determining the folding pattern of a
- How do hydrophobic and hydrophilic residues arrange themselves in globular proteins
- How do peptides react with cyanogen bromide
- Describe the structure of a peptide giving the sequence
- What are some commonly used biochemical buffers
- How does isoelectric focusing work
- How does the UV absorption of specific amino acids aid biochemists
- How are free energy changes related to Lech atelier's Principle
- What are the axes of a Ramachandran plot, and what does it show us
- What factors are involved in determining the electrophoretic mobility of a molecule
- What is anti infective vitamin
- What is guaiac test and where it is used
- What is Ampholyte
- Explain the basic structure of collagen
- What is the composition of Adenyl cyclase
- What are Cabot rings and when are they found in body
- What is the Best Test Of Blood Glucose Estimation
- What is the structural formula of molybdenum blue
- Are glycine and Tyrosine hydrophobic or hydrophilic
- Which fat soluble vitamin has co-enzymic function
- Explain the Fermentation
- What are the factors affection Respiration
- How many types of Respiration explain them
- Explain about RESPIRATION
- When starch reacts with iodine, why does it create the characteristic blue-black
- Is there a biochemical test for maltose
- Some proteins profoundly alter the structure of DNA when they bind, bending it far
- Many genes are regulated in both a negative and a positive manner. The genes
- Compare and contrast feedback inhibition and enzyme repression
- What is Alzheimer's disease?what are its symptoms
- What is the role of PAPS
- What is a plasma logen? What do plasma logens do
- "Wobble" hypothesis means
- What is RFLP
- What is a transcription factor
- What is xeroderma pigment osum
- What is the primosome
- Distinguish between type I and type II DNA topoisomerases
- What is dsDNA said to be anti parallel
- Compare endonuclease and exonuclease
- What are some common modifications made to sugars in GAGs
- What are proteoglycans and how are they constructed
- How is glycogen synthesized
- Where is lactose mainly produced in mammals
- What is the importance of sorbitol
- How to name a glycosidic bond
- What are Epimers
- What are carbohydrates used for in living systems
- What is the difference between aldose and a ketose? Give an example of each
- When a forensics laboratory tests evidence collected at the scene of a crime using
- Which compound is involved in reducing levels of homo cysteine in the blood
- Which organ and sub cellular site are most important for fatty acid bio synthesis
- Reduction of which intermediate in glycolysis leads directly to a compound involved
- Which vitamins participate, in coenzyme form, in reactions of the tricarboxylic acid
- During a heart attack, blood flowing to the heart muscle is interrupted by blockage
- Name the terminal electron acceptor during mitochondrial respiration
- What is the primary purpose of fermentation in the absence of oxygen
- Which cellular compartment becomes acidic during mitochondrial electron transport
- Explain why in anaerobic cells the ratio of pyruvate/ lactate is much less than 1
- If you isolate mitochondria and place them in buffer with a low pH they begin to
- Why does the pH of the blood decrease in a person who has digested trematol
- Why does physical exertion increase symptoms of poisoning by trematol
- What determines whether a B-cell will respond to an antigen
- Two children have a neurological disorder. When cells from the two patients were
- What will happen to a mixture of monomeric alpha and beta chains of hemoglobin at
- Which vitamins participate in co-enzyme form in reactions of Tricarboxylic acid cycle
- What is nanotechnology
- What are angiotensins
- What is zone electrophoresis
- What are the drawbacks of tissue slices technique
- What is the use of sephadex in ion exchange chromatography
- What are the hormones secreted from Crustaceans
- What is cellobiose what are its important properties
- What is the difference between reducing sugars and non reducing sugars
- What is the composition of agent orange
- What is the difference between chvostek's sign and trousseau's sign
- How I cell disease is caused
- What are wood-werkmann's reactions
- How the keratosulphate differs from other muco polysaccharides
- What are the two types of intermediates
- Name amino acids which contains sulfur
- What is the structure of cerebroside
- What are the reasons for gaucherie's disease
- What is schweizner's reagent
- What are 3 types of plasmalogens
- Name the 3 hormones present in urine of pregnant women
- What are the two types of methylmalonic academia
- What is kallidin
- What is the difference between angiotensin-1 and angiotensin-2
- What is the functionality of bongkrekat
- What are lac operons
- What is a Reducing sugar
- What are char gaff's equivalence rules
- Chemical structure of trehalose
- How papaverine can be prepared from tyrosine
- How the nucleoside analogues are used as drugs
- What are the two renal hormones
- How rote none acts as an inhibitor of electron transport
- What is the difference between alpha carotene and beta carotene
- What is the importance of nigericin
- What is polenske number
- What is MSG
- What is familiar hyper cholesterol emia
- What are the two imp characters of nitrogenous complex
- What is the chemistry of cellulose
- What is lobry debrugn alberda van ekenstein transformation
- How waxes can be prepared
- What are the two cellulose derivatives used for protein purification
- What is the chemical formula for cholesterol
- What is the difference between MUFA and PUFA
- Which is anti egg injury factor
- Which is called as mouse antilopecia factor
- What is the test which is specific for tyrosine
- What are hetero polysaccharides
- What are the two mixed triglycerides
- Which is known as anti dermatitis factor
- Hormones from echinodermata
- What is the structure of colip's hormone
- What is the amino acid sequence of Brady kin in
- What is the important source for drug diosgenin
- What is informosome
- What are the different types of monoterpenes
- How do the two components of starch differ
- Which is known as invert sugar
- What are hydrophobic interactions
- What are the different types of calines
- Which is known as biologic grignard reagent
- What are bioflavinoids
- What are the salient features of chemiosmotic coupling hypothesis
- What is non competitive inhibition
- What are anaplerotic pathways
- Which solvent mixture is normally used in paper chromatography
- What is the difference between Dowex-1 and Dowex-50 which are used in ion exchange
- What is the structure and function of pellagra-preventive factor
- What are endorphins
- What are the symptoms of Adrenal Virilism
- What is Signal Recognition Particle
- How streptomycin acts an inhibitor for protein synthesis
- What is meant by Shine-Dalgarno sequence in protein synthesis
- What is the concept behind central dogma of molecular genetics
- What is albinism
- What are low-density lipoproteins?what are their functions
- What happens when amino acid reacts with edman reagent
- What is the structure and metabolism of ALPHA-LIPOIC acid
- What is castration process
- The peptide bond in proteins is
- The nucleophile in the first stage of the serine protease mechanism is
- The elution volume of an enzyme on a gel filtration column can be predicted from
- DNA binding by proteins with the helix-turn-helix (HTH) motif does not involve
- The two exonuclease activities of DNA polymerase I
- A principal difference between prokaryotic and eukaryotic DNA replication is
- When s subunit dissociates from an initiated RNA polymerase
- The junction between the two helical portions of tRNA is stabilized by many non
- When it functions as a "second messenger", cAMP
- The reduction-oxidation (Redox) potentials of NADH and FADH2 show that the following
- The ATP synthase of bacteria is an Fl-like particle attached to the
- The yield of ATP/glucose unit in glycolysis with glycogen as the glucose source is
- What was the primary antibody that was used
- Why do proteins that recognize specific DNA sequences usually bind in the major
- Splicing of pre-mRNA involves an unusual phosphodiester bond. Why is it unusual
- Review your data from the entire module. Say we ask you to redo the purification
- According to the fluid mosaic model of cell membranes, which type of molecule spans
- If the enthalpy change for a reaction is zero, DG? is equal to
- What are magic 20 amino acids
- What is racemic mixture and what is racemisation
- An unusual structure is formed at the 5 end of each cellular mRNA. What is it? After
- What is the difference between C-DNA and D-DNA
- What is acid number
- What is the action of dicoumarol
- What is le bel-van?t Hoff rule
- What is the importance of metabolic water
- What is the chemical structure of hyaluronic acid
- What are Neurotransmitters
- Explain the principle of ultra centrifuge
- What is the ping-pong mechanism regarding to enzyme reactions
- How histidine is synthesised
- What is the opposing rolling circle model of DNa
- How do u synthesise phenanthrene alkaloids
- What are the common features of active site
- What are isozymes
- Explain Cloverleaf model of the t-RNA base sequence of yeast alanine
- What is the phenomenon of Acrolein test
- What are the two types of confirmation of a cyclohexane ring
- What is the difference between Phospholipids and phosphosphingosides
- What is meant by non-conjugated double bond system
- What is the product formed when aminoacid reacts with benzaldehyde