-ase, -tase tips - ANS-if some thing ends with -ase (ex: synthase), it's miles an enzyme.
If something ends with -tase (ex: synthetase), it's miles an enzyme which uses electricity (like
ATP). Be careful due to the fact a few enzymes which use energy can practice to reversible
reactions and despite the fact that energy is utilized in going handiest one manner, it
nonetheless has the -tase finishing.
6 Molecular interactions that make a contribution to a tertiary protein structure - ANS-1)
HYDROGEN BONDING between N-H and C=O or aspect chains (amine, carboxyl, and alcohol
companies)
2) DISULFIDE BONDS - covalent bond among 2 cysteine residues
three) HYDROPHILIC/HYDROPHOBIC INTERACTIONS- in soluble proteins, hydrophobic
amino acids disintegrate into the protein core. In membrane proteins, hydrophilic membranes
could be out of doors the membrane in the cytoplasm or in the middle of the protein.
Hydrophobic amino acids will be positioned in the bilayer.
4) IONIC INTERACTIONS - charge-price interactions among a undoubtedly charged amino acid
(ex: lysine) and a negatively charged amino acid (aspartic acid) (NH3+ R institution interacting
with COO- R organization - no longer the zwitterion element)
5) VAN DER WAALS FORCES - intermolecular forces that repel atoms far from every different
(steric challenge)
6) PROLINE TURNS - proline's unusual shape will reason a KINK in the center of an alpha
helix, but it aids in beta turns (see proline)
Absolute Configuration - ANS-L or D designations are given based totally on which aspect of the
Fischer Projection an Amine institution is.
ALL HUMAN AMINO ACIDS ARE L as they're derived from L-Glyceraldehyde
All amino acids apart from Cysteine (R) and Glycine have an S stereocenter
Active Site - ANS-region on the enzyme wherein the substrate binds.
Aldose vs. Ketose Distinctions - ANS-You can inform a ketose from an aldose in a sequence
shape due to the presence of a ketone purposeful organization instead of an aldehyde
purposeful institution (Fischer projection). In ring form, you could inform via searching out R
companies on BOTH facets of the hoop oxygen. If , as in fructose, you notice an R-OH group
attached to the carbons on BOTH sides of the hoop oxygen, then you understand it's far a
KETOSE. On the alternative hand, if, as in glucose, ONE facet has an R-OH institution and the
other has ONLY an -OH organization, then it must be an ALDOSE.
,Allosteric enzymes - ANS-enzymes whose hobby is encouraged through the reversible,
non-covalent, bonding of another molecule (i.E. Second subunit or an activating/deactivating
molecule). Ex: Threonine deaminase is an allosteric enzyme. It has 2 binding web sites. When
isoleucine binds to the excessive affinity website online, binding affinity for the low affinity web
page increases (some thing else will bind there to spark off it). If isoleucine binds to the low
affinity website, the enzyme deactivates.
Alpha Carbon Stereocenter - ANS-All human amino acids are chiral EXCEPT for GLYCINE.
They have an R organization, a hydrogen, a Carboxylic acid, and an amine.
Alpha Helices - ANS-Hydrogen bonding among CARBONYNL OXYGENS and AMIDE
HYDROGENS that are exactly FOUR is living apart.
ONLY each FOURTH residue is worried in hydrogen bonding
R companies are directed exactly far from the alpha helix cylinder (i.E. Perpendicular to a
aircraft tangent to the floor of the alpha helix)
Anomers - ANS-SAME molecule; specific stereochemistry at the anomeric carbon
Anomeric carbon = carbonyl carbon inside the Fischer projection
Apoenzyme - ANS-SIMPLE PROTEIN that is an ENZYME
Basic Kinetics Formula - ANS-E + S <--> ES --> EP <--> E + P
Beta Pleated Sheets - ANS-Hydrogen bonding among ALL of the CARBONYL OXYGENS in
one row and the AMIDE HYDROGENS within the adjoining row.
ALL residues are worried in hydrogen bonding
R organizations are directed perpendicular to the plane of the beta sheet, on both sides.
Beta sheets are in a PLEATED conformation. This is vital for the carbonyl and amide moties to
line up well so that EVERY RESIDUE is collaborating in TWO HYDROGEN BONDS.
Buffer Region - ANS-The location of a titration curve wherein the attention of a conjugate acid is
about equal to that of the corresponding base. The pH remains quite constant while small
amounts of H+ or OH- are added due to the aggregate of those ions with the buffer species
already in solution.
FLAT part of a titration curve
Carbohydrate Empirical Formulas - ANS-Empirical system of all monosaccharides = (CH2O)n
, Empirical formula of all polysaccharides = Cn(H2O)x
Carbohydrate Nomenclature and Classification - ANS--"-ose" finishing is given to all sugars (i.E.
GlucOSE, ribOSE)
-"deoxy-" prefix is used inside the regular location of an -OH institution is replaced with
Hydrogen (i.E. DNA vs. RNA)
Aldose vs. Ketose (aldehyde vs. Ketone)
Carbohydrate Reactions: Hydrolysis of the Glycoside Linkage - ANS-Using water to interrupt
polymers.
Polymer (n) + H2O --> Polymer (n-1) + Monomer
Carbohydrate Reactions: Ring Closing - ANS-INTRAMOLECULAR NUCLEOPHILIC
SUBSTITUTION: The -OH group on te chiral caron this is furthest fromt eh carbonyl carbon (the
identical one used to determine D/L) acts as the nucleophile, attacking the carbonyl carbon
(electrophile). The carbonyl oxygen is protonated to shape a hydorxyl institution.
Central Dogma - ANS-DNA --> RNA --> Proteins
DNA and RNA has NUCLEIC ACID constructing blocks
Proteins have AMINO ACID building blocks
Chymotrypsin (protein hydrolysis) - ANS-cleaves PHENYLALANINE, TRYPTOPHAN, and
TYROSINE on the CARBOXYLIC aspect.
Think of the R-Groups with aromatic jewelry
It is made from Serine, Histidine, and Aspartate
Coenzymes - ANS-Non-Protein species TEMPORARILY connected to the enzyme but
REQUIRED by way of the enzyme to function
Cofactors - ANS-preferred term for any species required via an enzyme to characteristic;
coenzymes and prosthetic groups are both examples of cofactors
Common programs of secondary Structures: Fibroin - ANS-molecule that makes up silk = beta
sheets
Common applications of secondary Structures: Keratin - ANS-found in hair and nails = alpha
helices