Online Biochem

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59 Terms

1
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What is the angle of a sp3 bond?

109.5

2
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What are the major elements in living organisms?

H,C,N,O,Na,P,S,Cl,K,Ca

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What are the angles in a sp2 bond?

120

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What shape are sp2 bonds?

Planar trigonal

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What the angles in a sp bond?

180

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Stereoisomer

Same composition but a different configuration

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Configurational isomer

Different arrangements of groups around a chiral center, a single bond must break

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Enantiomers

Mirror images, can never be rotated to get the other enantiomer (a bond must break)

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Confromations

From rotation around a single bond

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Eclipsed

Higher energy, less stable

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Staggered

Lower energy, more stable

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Configuration

Fixed arrangement of atoms directed by the bonds of a molecule

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Biochemical reactions

Matter and energy exhanged

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Catabolism

Converting energy to be used

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Why does energy need to be convereted?

To do work and anabolism

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Phototroph

Uses sunlight as energy

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Chemotroph

Energy from chemical molecules

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Lithotroph

Inorganic molecules used as fuel

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Organotroph

Organic molecules are used as fuel

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Autotroph

Fix CO2 to get carbon

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Heterotroph

Use organic molecules to get carbon

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Energy

The capacity to do work

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What is the first law of thermodynamics

Energy is constant, never created or destroyed, only changes forms

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What is the second law of thermodynamics?

Energy is transferred to increase entropy

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What is gibbs free energy equation?

G=H-TS or DG=-RTln(keq)

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Enthalpy

Total energy in a system

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Free energy

Energy available to do work

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Spontaneous

Negative DG, exergonic, DH<TS, energy released, products more stable than reactants

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Nonspontaneous

Endergonic, positive DG, products less stable than reactants

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Equilibrium

No net change between products and reactants, no work is done

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What is the equation to find the equilibrium constant?

K=[P]/[R]

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Le Chateliers principle

When equilibrium is disturbed, the system will correct this change and move back to equilibrium

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Draw the structure of an amino acid

knowt flashcard image
34
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Zwitterion

Has a positive and a negative charge

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Why does binding need energy input?

Due to loss of entropy

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Sulfhydryl

Very reactive, forms disulfide bonds in extracellular conditions

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Where do disulfide bonds form?

In extracellular conditions (oxidizing), inside of cells it is reducing

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Glycine

Not chiral, important for folding

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Proline

Cyclic, conformationally restricted

40
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What are the types of secondary structures of proteins?

Helix, beta sheet, and loop

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How do peptide bonds form?

Condensation reaction

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Peptide bond

Unbranched, planar, no rotation, must be cis or trans

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Is cis or trans favored for a peptide bond?

Trans, except when proline is the terminal amino acid

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Phi

Bond between N and the alpha C

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Psi

Between carbonyl carbon and alpha carbon

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How are phi bonds measured?

Look down the bond from the N to the terminal alpha carbon, then measure the angle between the carbonyl carbons

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How are psi bonds measured?

Look down N to the terminal alpha carbon, measure the angles between the Ns

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Ramachadran plot

Areas of dihedral angles that phi/psi that are allowed for regular proteins, have minimized steric clashses

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What allows secondary structures to form?

Multiple bonds in a row being in the same plot area, polar groups forming H-bonds

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Helix

carbonyl of x bonds with the amino group of x+4, 3.6 residues per turn, side chains point out

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Beta sheet

Multiple beta strands joined through H-bonds, side chains perpendicular to H-bonds, can be parallel anti parallel or both, sides of sheets have different properties

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Loop

Can be any combination of plot areas, connect secondary structures, many small and polar residues, form active sites, flexible, proline and glycine here often

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How are peptide bonds named?

Cis (0) and trans (180)

54
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Alcohol dehydrogenase

Enzyme that is important in energy metabolism

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Primary structure

Amino acid sequence

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What geometry does an alpha carbon have?

Tetrahedral

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What geometry does a carbonyl carbon have?

Trigonal

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What atoms connect to form a peptide bond?

Carbonyl carbon and nitrogen

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Imino acid

R group connects with N and carbonyl C, no h to h bond with, breaks alpha helixes