Foundations Exam Part 1 Flashcards
What are some examples of lipids in the body?
Fatty acids, cholesterol, and other hydrophobic molecules
What is the most essential component of a cells membrane?
The phospholipid
What is the definition of an epimer?
Diastereomers whose configuration differs only at one asymmetric carbon
Aldoses and ketoses form ________
cyclic structures
Glucose cyclizes to form Two Pyranose Ring Structures
These are called _______-type diastereomers
Anomer-type Diasteromers
Alpha-anomer has -OH at C-1 on ________ side of ring from -CH2OH at chiral carbon atom that determines ____ or ____ configuration
Alpha-anomer has -OH at C-1 on OPPOSITE side of ring from -CH2OH at chiral carbon atom that determines D or L configuration
Beta-anomer has -OH on the ____ side of ring as the CH2OH at the chiral carbon atom
Beta-anomer has -OH on the SAME side of ring as the CH2OH at the chiral carbon atom
D-Fructose Cyclizes to a 5-membered ______ ring structure
Furanose
List the Purines
Adenine and Guanine
LIst the Pyrimidines
In DNA: Thymine and Cytosine
In RNA: Uracil and Cytosine
Definition: Base attached to a pentose sugar
Nucleoside
Definition: Monophosphate, diphosphate, and triphosphate of esters of nucleosides
Nucleotide
A-T base pairs form ______ hydrogen bonds
A-T base pairs form 2 hydrogen bonds
G-C base pairs form _____ hydrogen bonds
GC base pairs form three hydrogen bonds and are more stable than AT-rich regions
Proteins are ______ chains of _______ covalently linked amino acids
Proteins are linear chains of COVALENTLY linked amino acids
Polypeptide chains are directional and the chains are denoted from ____ to _____ end
Polypeptide chains are directional and conventionally chains are denoted from N to C end.
Secondary structures of proteins entail
alpha helixes (side chains are on the outside of the helix)
Beta strands align in parallel or antiparallel orientation to form Beta sheets
Hydrogen bonding rich in secondary structures
In tertiary structures of proteins, what is the folding driven by?
Folding is driven by the burial of hydrophobic residues from water
Where do proteins undergo post-translational modification?
In the ER and Golgi body proteins under post-translational modification
What is Glycosylation?
Glycosylation is a form of protein modification in the secretory pathway.
Secretory proteins have a signaling sequence at the beginning of them
What are Signal recognition particles and in what processes do we find them?
SRPs bind to signaling sequences in glycosylation. Glycosylation is a form of post-translational modification.
SRP binds to receptors on the endoplasmic reticulum and move protein through pores in the ER.
Where does glycosylation occur?
Glycosylation occurs in either the ER or the Golgi.
What are the roles of glycosylation?
-N linked on asparagine, O-linked on Serine
-Assists in protein folding to reach the correct shape
-Enhance protein solubility
-Stabilize the protein against denaturation
-protect the protein from proteolytic degradation
-target the protein to specific subcellular locations
-Serve as a recognition signal for carbohydrate-binding proteins (lectins) or provide special properties
Write out the answers to the following questions
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