You are in browse mode. You must login to use MEMORY

level: Level 1

Questions and Answers List

level questions: Level 1

Question	Answer
Final shape or structure of polypeptide chain	Protein Conformation
The amino acid in a protein	Residue
The R-Group.	Protein Side Chain
Non-R Group parts of a protein	Protein Backbone
The Amino Acid Terminus (beginning of backbone)	N Terminus
Carboxyl Terminus (End of Backbone)	C-Terminus
Short Protein	Peptide
Integral Proteins Cross the cell membrane Act as Pathways for ions and molecules	Transmembrane Protein
The Backbone Order of Amino Acids N-Terminus---(Peptide Sequence)---C-Terminus Peptide Bonds 1 chain	What is Primary Structure
The gene that corresponds to the protein	What determines the primary structure
The two Cs one attached to Carboxyl one attached to anime group The H and CH3 are R's (H-N-H) -N-term (O=C-OH) C-Term	ON Dipeptide label the following: Two central carbons, N-term, C-term, two R groups (H-N-H)-(H-C-H)-(C=O)-(N-H)-(H-C-CH3)-(O=C-OH)
Ribbon A-Helix and B-Sheet Hydrogen Bonds between Carbonyl of an amino acid with Amino H of another. A-Helix-- Spiral... Bond every t down B-Sheet--2 or more segments line up parrallel or anti parallel. 1 Chain	Secondary Structure
Wire Folds in protein due to interactions of R-Groups Covalent: Disulfide Bonds Non-Covalent: Hydrogen Bonds, Ionic Bonds, Hydrophobic Interactions 1 Chain	Tertiary Structure
Space-Filling folds in protein due to R Groups Disulfide, Hydrogen, Ionic, and Hydrophobic Bonds 2 Chains or More	Quaternary Structure
Oligomer with 2 subunits that may or may not be identical	Dimer
Oligomer with 3 subunits that may or may not be identical	Trimer
Oligomer with 4 subunits that may or may not be identical	tetramer
Oligomer with 4 different subunits	Heterotetramer
Oligomer with 3 identical subunits with same form and function	homotrimer
Protein in its 3D structure	Protein Domain
proteins that are structurally and functionally similar	Protein Family
e- donor; transmits signals between cells	Ligand
Having more than 1 conformation of shapes "off" and "on"	Allosteric
Ligand binds to Proteins by Weak Interactions Lock & Key or Induced P + L (ka)<--->(kd) PL	How do proteins interact with ligands?
Phosphorylation Allosteric Inhibition GTP-Binding ATP Hydrolysis	What are 4 ways that protein function is regulated?
Esterification rxn. happens after translation from RNA template Phosphoryl Group +(Enzyme: kinase) + (-OH) --->phosphoryl group-OH Reverse Rxn: Dephosphorylation: Phosphoryl group -OH + phosphatases ----> Phosphoryl group + (-OH)	Phosphorylation
A non-competitive inhibitor which attaches to the enzyme at allosteric site i.e any place on enzyme except active site, is called allosteric inhibitor.	Allosteric Inhibition
During the elongation stage of translation, GTP is used as an energy source for the binding of a new amino bound tRNA to the A-site of the ribosome.	GTP BINDING
ATP + H2O <=> ADP + inorganic phosphate (Pi)	ATP Hydrolysis
The process of gene information turns into a gene product	Gene Expression
Enzyme that catalyzes the synthesis of RNA from DNA	RNA Polymerase II
Step where DNA is Copied to Form an mRNA template	Transcription
5' Capping to 3' Cleavage to Polyadenylation + RNA Splicing Modification made to RNA between its transcription	RNA Processing
Where Transcription starts 5' End of gene sequence	Start Site
First codon with 3 Nucleotide sequence of an mRNA translated by ribosome (AUG)	Start Codon
Step RNA to Protein. Protein is synthesized by mRNA info.	Translation
3 nucleotide sequence of DNA or RNA	Codon
3 nucleotide sequence in tRNA that identifies the amino acid that carries to and binds to a comp. codo in mRNA.	Anticodon
Genetic info flow from DNA to RNA and RNA to Protein. Replication-Transcription-Translation.	Central Dogma
Their Gene Expression is different therefore the protein functions are different.	What makes one type of cell different from another even if they have the same genome?
DNA-RNA 1. Structure- double stranded--single stranded 2. Function- replicates and stores genetic info. --converts genetic info into proteins 3. Sugar- one less hydroxyl group from ribose- has ribose 4. Base Pairs - A-T/C-G -- A-U/C-G	4 ways DNA is different from RNA
messenger RNA- transfers Genetic info from Genes to Ribosomes to synthesize Proteins	mRNA
transfer RNA- transfers amino acid to mRNA	tRNA
Ribosomal RNA- provides structural framework for RNA	rRNA
involved in mRNA processing	snRNA
1. Gene Expression- DNA copied to mRNA 2. RNA polymerase binds to sequence of gene 3. Uses 1 DNA strand as template to make complimentary RNA 4. Ends when RNA polymerase crosses STOP sequence in gene	Describe Transcription
1. Addition of 5' Cap 2. Addition of 3' polyadenylation tail 3. RNA Splicing- protons are remove, exons are joined prior to translation.	Describe 3 parts of RNA Processing
Protein synthesis from RNA 1. initiation-ribosomal subunit binds to START of mRNA seq. 2. tRNA carries amino acid METH. 3. Start codon of mRNA seq 4. Ends when Ribosome reaches STOP codon (UAA, UAG, UGA)	DescriBe Translation
P-peptidyl site -binds to trna -polypeptide chain A-Acceptor Site -binds to aminoacyl trna - new amino acid E-Exit Site - threshold---before amino acid is "let go"	What are EPA sites