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match the following words and definitions correctly. Prion Phenylisothiocyanate

ID: 147117 • Letter: M

Question

match the following words and definitions correctly.

Prion

Phenylisothiocyanate

Hill plot

Cofactor

Binding energy

Feedback inhibition

Motif

NMR

Sigmoid

Active site

Covalent catalysis

Consensus sequence

Ramachandran diagram

Assay

fMRI

Induced-fit

Recognition sequence

Zymogen

L-amino acid

Chromatography

Heme

Transition state analog

Methylase

Homotropic effect

Zwitterion

Homogenate

R-state

Michaelis-Menten Constant

ATPase

Protein kinase A

The restriction of an enzyme by the end-product of a metabolic pathway.

Compounds proposed by Dr. Linus Pauling to be very effective inhibitors of enzymes.

Ratio of rate constants for monoenzyme:monosubstrate complexes.

2-D plot of allowed angle of rotation values for phi and psi bonds.

Reacts with the uncharged terminal amino group of a peptide.

Cellular protein found in the brain.

The inactive precursor of an enzyme.

Small molecules needed for the catalytic activity of many enzymes.

Complementary shape assumed only after the substrate is bound to the active site of some enzymes.

Consist of organic and inorganic components; gives blood and muscle their distinctive red color.

Free energy released in the formation of a large number of weak interactions between the enzyme and the substrate.

Targeted recognizable protein sequence.

One of two mirror-image alpha amino acids that are constituents of proteins.

The separation of a mixture by passing it in solution or suspension or as a vapor (as in gas chromatography) through a medium in which the components move at different rates.

Cellular mixture after cell membrane disruption.

Detects changes in an organ mediated by changes of magnetic properties.

Enzymes that add single carbon alkyl groups to adenine bases in host DNA.

Enzymes that alter the activities of target proteins by adding a phosphate to specific serine or threonine residues.

Relaxed state of the quaternary structure of a cooperative binding molecule.

Reveals atomic structure of a high concentration of a macromolecule less than 15 kD in solution.

Dipolar amino acids that exist in solution at neutral pH.

Particular nucleotide sequences recognized by restriction endonucleases.

Catalyses the hydrolysis of adenosine triphosphate.

A test that takes advantage of a protein's unique identifying properties and used during the purification process.

Enzymatic reactions that usually involve a powerful nucleophile that becomes temporarily covalently attached to a part of the substrate.

Certain combinations of secondary structure present in many proteins; exhibit similar functions.

Description of a cooperative binding curve with an "S" shape.

The region of an enzyme that binds the substrate(s) and cofactor, if any.

A useful way to quantitatively describe the cooperative binding process.

Action of substrates on allosteric enzymes.v

Prion

Phenylisothiocyanate

Hill plot

Cofactor

Binding energy

Feedback inhibition

Motif

NMR

Sigmoid

Active site

Covalent catalysis

Consensus sequence

Ramachandran diagram

Assay

fMRI

Induced-fit

Recognition sequence

Zymogen

L-amino acid

Chromatography

Heme

Transition state analog

Methylase

Homotropic effect

Zwitterion

Homogenate

R-state

Michaelis-Menten Constant

ATPase

.

Protein kinase A

A.

The restriction of an enzyme by the end-product of a metabolic pathway.

B.

Compounds proposed by Dr. Linus Pauling to be very effective inhibitors of enzymes.

C.

Ratio of rate constants for monoenzyme:monosubstrate complexes.

D.

2-D plot of allowed angle of rotation values for phi and psi bonds.

E.

Reacts with the uncharged terminal amino group of a peptide.

F.

Cellular protein found in the brain.

G.

The inactive precursor of an enzyme.

H.

Small molecules needed for the catalytic activity of many enzymes.

I.

Complementary shape assumed only after the substrate is bound to the active site of some enzymes.

J.

Consist of organic and inorganic components; gives blood and muscle their distinctive red color.

K.

Free energy released in the formation of a large number of weak interactions between the enzyme and the substrate.

L.

Targeted recognizable protein sequence.

M.

One of two mirror-image alpha amino acids that are constituents of proteins.

N.

The separation of a mixture by passing it in solution or suspension or as a vapor (as in gas chromatography) through a medium in which the components move at different rates.

O.

Cellular mixture after cell membrane disruption.

P.

Detects changes in an organ mediated by changes of magnetic properties.

Q.

Enzymes that add single carbon alkyl groups to adenine bases in host DNA.

R.

Enzymes that alter the activities of target proteins by adding a phosphate to specific serine or threonine residues.

S.

Relaxed state of the quaternary structure of a cooperative binding molecule.

T.

Reveals atomic structure of a high concentration of a macromolecule less than 15 kD in solution.

U.

Dipolar amino acids that exist in solution at neutral pH.

V.

Particular nucleotide sequences recognized by restriction endonucleases.

W.

Catalyses the hydrolysis of adenosine triphosphate.

X.

A test that takes advantage of a protein's unique identifying properties and used during the purification process.

Y.

Enzymatic reactions that usually involve a powerful nucleophile that becomes temporarily covalently attached to a part of the substrate.

Z.

Certain combinations of secondary structure present in many proteins; exhibit similar functions.

AA.

Description of a cooperative binding curve with an "S" shape.

AB.

The region of an enzyme that binds the substrate(s) and cofactor, if any.

AC.

A useful way to quantitatively describe the cooperative binding process.

AD.

Action of substrates on allosteric enzymes.v

Explanation / Answer

Prion - F

Phenylisothiocyanate - E

Hill plot - AC

Cofactor- H

Binding energy - K

Feedback inhibition - A

Motif - Z

NMR- T

Sigmoid - AA

Active site - AB

Covalent catalysis - Y

Consensus sequence - L

Ramachandran diagram - D

Assay - X

fMRI - P

Induced fit - I

Recognition sequence - V

Zymogen G

L-amino acid - M

Chromatography - N

Heme - J

Transition state Analog - B

Methylase - Q

Homotropic effect - AD

Zwitter ion - U

Homogenate - O

R state - S

Michaelis-Menten constant - C

ATPase - W

Protein kinase A - R