Bio Chem Chapter 4

Front 1

2, 3-bisphosphoglycerate (2,3-BPG)

Back 1

Enhance delivery of oxygen by hemoglobin

Front 2

Allosteric Effector or Modulator

Back 2

A biomolecule that binds to the regulatory site of an allosteric protein and thereby modulates its activity

Front 3

Allosteric Interaction

Back 3

The modulation of activity of a protein that occurs when a molecule binds to the regulatory site of the protein

Front 4

Allosteric Protein

Back 4

A protein whose activity is modulated by the binding of another molecule

Front 5

Bohr Effect

Back 5

The phenomenon observed when exposure to carbon dioxide, which lowers the pH inside the cells, causes the oxygen affinity of hemoglobin in red blood cells to decrease

Front 6

Carbamate Adduct

Back 6

Carbon dioxide is carried in the hemoglobin in this form

Front 7

Conformation

Back 7

any three-dimensional structure, or spatial arrangement, of a molecule that results from rotation of functional groups around single bonds. Can assume many of these

Front 8

Cooperativity of Folding

Back 8

The phenomenon whereby formation of structure in one part of a macromolecule promotes the formation of structure in the rest of the molecule

Front 9

Denaturation

Back 9

A disruption in the native conformation of a biological macromolecule that results in loss of the biological activity of the macromolecule

Front 10

Domain

Back 10

A discrete, independent folding unit within the tertiary structure of a protein. Combinations of several motifs

Front 11

Fibrous Protein

Back 11

A major class of water-insoluble proteins that associate to form long fibers. Physically tough and provide mechanical support

Front 12

Fold

Back 12

A combination of secondary structures that form the core of a protein domain

Front 13

Globular Protein

Back 13

A major class of proteins, many of which are water soluble. Compact and roughly spherical, containing tightly folded polypeptide chains

Front 14

Hairpin Loop

Back 14

A secondary structure adopted by single-stranded polynucleotides that arises when short regions fold back on themselves and hydrogen bonds form between complementary bases

Front 15

Heat Shock Proteins

Back 15

A protein whose synthesis is increased in response to stresses such as high temperature. many are chaperones

Front 16

Loop

Back 16

A non-repetitive polypeptide region that connects secondary structures within a protein molecule and provides directional changes necessary for a globular protein to attain its compact shape

Front 17

Molecular Chaperone

Back 17

A protein that forms complexes with newly synthesized polypeptide chains and assists in their correct folding into biologically functional conformations

Front 18

Monomer

Back 18

A small compound that becomes a residue when polymerized with other monomers

Front 19

Motif

Back 19

A combination of secondary structure that appears in a number of different proteins

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Oligomers

Back 20

A multi subunit molecule whose arrangement of subunits always has a defined stoichiometry and almost always displays symmetry

Front 21

Oxygenation

Back 21

The reversible binding of Oxygen to a macromolecule

Front 22

Peptide Group

Back 22

The nitrogen and carbon atoms involved in a peptide bond and their four substituents; the carbonyl oxygen atom, the amide hydrogen atom, and the two adjacent a-carbon atoms

Front 23

Pitch

Back 23

The axial distance for one complete turn of a helical structure

Front 24

Positive cooperativity of binding

Back 24

There is one binding site per subunit for each ligand, that the conformation of each subunit is constrained by its association with other subunits

Front 25

Primary Structure

Back 25

The sequence in which residues are covalently linked to form a polymeric chain

Front 26

Proteomics

Back 26

the entire complement of proteins that is or can be expressed by a cell, tissue or organism

Front 27

Quaternary Structure

Back 27

The organization of two or more polypeptide chains within a multisubunit protein

Front 28

R State

Back 28

One conformation of Hemoglobin, facilitates oxygen binding oxy conformation

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T State

Back 29

One Conformation of Hemoglobin which resists oxygen binding deoxy conformation

Front 30

Secondary Structure

Back 30

is maintained by hydrogen bonds between carbonyl carbons and amide groups of the backbone.

Front 31

Tertiary Structure

Back 31

The compacting of polymeric chains into one or more domains within a macromolecule. Stabilized by hydrophobic interactions between side chains

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Turns

Back 32

Short loops of up to 5 residues

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Alpha helix

Back 33

A common secondary structure of proteins, in which the carbonyl oxygen of each amino acid residue forms a hydrogen bond with the amide hydrogen of the fourth residue further toward the C-terminus of the polypeptide chain

Front 34

B-pleated Sheet

Back 34

Planar peptide group meet each other at angles like the folds in an accordion

Front 35

B sheet

Back 35

A common secondary structure of proteins that consists of extended polypeptide chains stabilized by hydrogen bonds between the carbonyl oxygen of one peptide bond and the amide hydrogen of another on the same or an adjacent polypeptide chain. Nearly perpendicular which may be parallel or antiparallel

Front 36

B strand

Back 36

An extended polypeptide chain within a B sheet secondary structure or having the same conformation as a strand within a B sheet