protein engineering 🤡🤡🤡🤡🤡🤡 Flashcards

1
Q

antigen

A

Molecules that cause an immune response (recognized and bound by antibodies)

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2
Q

antibodies

A

Proteins of the immune system that recognize and bind to foreign molecules

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3
Q

phage display library

A

collection of bacteriophage particles that have segments of foreign proteins protruding from their surface

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4
Q

combinatorial library

A

Large series of related molecules that have been systematically generated by combining chemical groups and/or molecular motifs

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5
Q

alternative splicing library

A

Library of gene or protein sequences generated by randomized inclusion or exclusion of exons from an original protein

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6
Q

combinatorial screening

A

Screening of a large series of related molecules for those with useful properties

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7
Q

random shuffling library

A

Library of gene or protein sequences generated by randomized shuffling and linking of short segments

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8
Q

How are protein libraries created?

A

DNA is chemically synthesized and then the modules are assembled to give new artificial genes with PCR methods (usually overlapping primers).

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9
Q

DNA shuffling

A

Method of artificial evolution in which genes are cut into segments that are mutagenized, mixed, shuffled, and rejoined - trying to generate novel or improved protein activities.

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10
Q

epitopes

A

Localized regions of an antigen to which an antibody binds

BODER DEF: peptide sequence for which a monoclonal antibody will bind to (a flag so antibodies can recognize)

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11
Q

How does recombining protein domains affect proteins?

A

Proteins have discrete domains with individual functions. Recombining domains from different proteins can generate hybrid proteins with novel combinations of properties.

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12
Q

Directed Evolution

A

Technique for enhancing or altering the original activity of an enzyme by randomly mutating the gene and then screening for the new activity - library construction

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13
Q

error-prone PCR

A

Type of PCR in which mutations are introduced at random during the amplification steps - used for random mutagenesis

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14
Q

tyrosyl-tRNA synthetase

A

e Enzyme that charges tRNA with tyrosine (mutated through site-specific directed evolution)

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15
Q

How is the industrial efficiency of proteins increased?

A

Some proteins are larger than necessary so extra sequences are removed and the protein is simplified.

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16
Q

How do manipulations to the protein active site alter the stability of the protein?

A

altering amino acids in and around the active site may change the specificity of an enzyme toward substrates or cofactors.

A cofactor is a non- protein chemical compound that is bound to a protein and is required for the protein’s biological activity.

17
Q

How can you increase protein stability with amino acids?

A

Replacing glycine with any other amino acid or increasing the number of proline residues in a polypeptide chain will increase stability.

18
Q

How do certain unstable amino acids affect protein stability?

A

High temperature or extreme pH can convert asparagine and glutamine amides to their corresponding acids. The replacement of a neutral amid by the negatively charged carboxyl negatively impacts structure and activity.

19
Q

disulfide bonds

A

A bond between two closely situated cysteine residues in a protein that stabilizes the tertiary structure

20
Q

Melting Temperature (Tm)

A

the temperature at which 50% of the protein is denatured