Proteins Flashcards
Are covalent bonds formed by the nucleophilic addition-elimination reaction
Peptide Bonds/Linkage
reaction of 2 amino acids involved in peptide bonds
Carboxylic Group and Amino Group
what are the different structural organization of proteins
Primary Structure
Secondary Structure
Tertiary Structure
Quaternary Structure
the reaction in peptide bonds release a molecular ______ as the by product
Water
determine how the protein folds and interacts at the other levels of interaction is in the ________ structure
Primary
the order of amino acids in peptide chain is in the _______ structure
Primary
a peptide bond has a partial _____ bond characteristic, therefore it is _______
double, rigid
______ structure are 2 dimensional structure formed due to ______ bonding between _____ of ______ group and ______ of the _____ group
Secondary, Hydrogen, Hydrogen, Amine, Oxygen, Carbonyl
______ is a spiral structure consist of tightly packed, coiled polypeptide backbone core.
Alpha (a) helix
Secondary structure are formed through _____ bonds between ________
Hydrogen, Backbone atoms
have extensive hydrogen bonding
Alpha (a) helix
a-helix have _____ per turn
3.6aa
a combination of secondary structural elements producing a specific geometric pattern or motifs
Supersecondary Structures
Supersecondary Structures are connected by ________
Loop regions
it primarily form the core region of the molecule
Supersecondary Structures
all of the peptide bond components are involved in hydrogen bonding
Beta (B) sheets
other name of B-bends
Reverse turn/ Beta (B) turns
in the B-sheets the surface are ______
Pleated
Beta (B) bends is composed of ______
4aa
________ is a reverse direction of the polypeptide chain that helps to form a ____________
Beta (B) bends, compact globular shape
_____________ structure have a loop or coil _______
Nonrepetitive secondary , conformation
Nonrepetitive secondary structure have less ______ structure
regular
______ usually contains many _____ and charged _____ acids
Beta (B) bends, polar, amino
alpha helix and beta sheet provide a _________ to the secondary structure
Stability
Nonrepetitive secondary structure is also called as?
Random coil
are the two structures that provide maximal hydrogen bonding
alpha helix and beta sheet
______ refers to both the folding of domains and to the final arrangement
Tertiary Structure
Tertiary Structure is stabilized by?
Disulfide bonds
Hydrophobic interactions
Hydrogen bonds
Ionic interaction (electrostatic attraction)
Tertiary Structure can be determined by the use of _________ and __________
X-ray crystallography and NMR Spectroscopy
what does NMR Spectroscopy stands for?
Nuclear Magnetic Resonance
______ is the fundamental functional and 3D structural units of polypeptides
Domains
_______ is the unfolding and disorganization of a proteins secondary and tertiary structure without the hydrolysis of peptide
Protein Denaturation
Protein Denaturation is often ________ and ______ from solution
Insoluble, Precipitate
what are the denaturing agents of Tertiary Structure?
SDS (Sodium Dodecyl Sulfate)
Urea
Guanidium Hydrochloride
in Guanidium Hydrochloride if detergent is charged, it can disrupts ________ interaction
Electrostatic
disrupts hydrophobic interactions
Guanidium Hydrochloride
_______ is where a-helices and B-sheets tend to make the polypeptide rigid
Fibrous Proteins
________ are usually structural proteins
Fibrous Proteins
Fibrous Proteins tend to be ______ and _______
long, thin
examples of Fibrous Proteins
Cytoskeleton Protein
Elastin
Collagen
Protein folding can occurs in _______ to _______
Seconds, Minutes
_______ is the result from the formation of secondary structure driven by the ________ effect
Protein folding, Hydrophobic
molecular chaperones is also known as
HSP ( Heat Shock Proteins)
what is the role of chaperones?
Interact with the polypeptide by binding hydrophobic regions
Helps proteins fold properly
______ contain short a-helices and B-sheets interspersed with randomly coiled regions
Globular proteins
Globular proteins have the following characteristics:
Compact
Spherical
Flexible
Globular proteins usually have ________ activity
Enzymatic
______ is the loss of biological activity
Denaturation
______ is where the activity regains
Renaturation
_______ reduce disulfide bridges to 2 sulfhydryl groups
B-mercaptoethanol
B-mercaptoethanol formula
HS-CH2-CH2-OH
what are the denaturing processes in tertiary structure?
Heat
Mechanical disruptions
Drastic pH changes
______ is the multimeric units of polypeptide chain
Quaternary Structure
Quaternary Structure commonly occurring examples
Dimers
Trimers
Tetramers
A ___________ consist of 4 polypeptide chains
Tetramers
________ shows positive cooperativity-binding of one oxygen increases the binding of the succeeding oxygen molecule.
Quaternary Structure
________ is an important characteristics and is the basis for classifying amino acids into the four groups
R groups
Acidic chain contains a _______ group
Carboxylate
Basic side chain contains an _____ amino group
Additional
Is the only sulfydryl (-SH) containing amino acid, and has chemical property not shared by the other.
Cysteine
_____ group can easily be oxidized to form a disulfide bond (-S-S-).
Sulfhydryl
Two cysteine molecules react readily to form a ______ compound called ______
Disulfide, Cystine
The disulfide is easily converted to -SH groups by the action of ______
Reducing agents
_______ and ________ are the structural isomers of each other and has a unique set of properties.
Glycylalanine and alanylglycine
An organic compound containing both an amino group and carboxylate group with the amino group attached to the carbon next to the carboxylate group
Alpha amino acid
Is derived from the word proteios, which means “of first importance”
Proteins
Indispensable components of all living things where they play crucial roles in all biological processes
Proteins
Each amino acid has a characteristics side chain or also known as ______ that imparts chemical individuality to the molecule
R groups
Acidic side chain contain _____ group in basic side chain contain ______ group
Carboxylate, additional amino
An amino acid polymer made up of more than 50 amino acid
Protein
