Study_Guide_3_Proteins - Study Guide 3 Proteins/structure...

Info iconThis preview shows pages 1–3. Sign up to view the full content.

View Full Document Right Arrow Icon

Info iconThis preview has intentionally blurred sections. Sign up to view the full version.

View Full DocumentRight Arrow Icon
This is the end of the preview. Sign up to access the rest of the document.

Unformatted text preview: Study Guide 3 Proteins/structure (Kopachik) Ch. 5 pp. 68-69, 77-86 Alpha (α) helix: a delicate coil held together by hydrogen bonding between every fourth amino acid Alpha carbon: the center of asymmetric carbon atom Amino acid: organic molecule possessing both an amino group and a carboxyl group Amino terminal end (N terminus): p80 Asymmetric carbon: attached to four different atoms or groups of atom Beta (β) sheet: two or more strands of the polypeptide chain lying side by side are connected by hydrogen bonds between parts of the two parallel polypeptide backbones Beta globin Carboxyl terminal end (C terminus): p80 Chaperonin (chaperon protein): protein molecules that assist in the proper folding of other proteins Contractile and motor protein: movement Defensive protein: protection against disease Dehydration (condensation reaction): monomers are connected by a reaction in which two molecules are covalently bonded to each other, with the loss of a water molecule, synthesizing a polymer Denaturation: if the PH, salt concentration, temperature, or other aspects of its environment are altered, the weak chemical bonds and interactions within a protein may be destroyed, causing the protein to unravel and lose its native shape Dimer Electrically charged R group: hydrophilic, R group has a second carboxyl or amino group usually on surface p79 Enzyme: catalyze chemical reaction function: molecules interact with one another and crystallize into a fiber; capacity to carry oxygen is greatly reduced Gene expression protein: Hormonal protein: coordination of an organism’s activities Hydrolysis: reverse of dehydration reaction, breaking down a polymer Methionine: Monomer: repeating units that serve as the building blocks of a polymer are smaller molecules Mutation: a change in the nucleotide sequence of an organism’s DNA or in the DNA or RNA of a virus Nonpolar R group: hydrophobic, usually found tucked away from protein surface p79 Peptide bond: the result of two amino acids are positioned so that the carboxyl group of one is adjacent to the amino group of the other, they can become joined by a dehydration reaction, with the removal of a water molecule Peptide: Polar R group: hydrophilic, with a polar group generally on protein surface, lot’s of hydrogen bond p79 Polymer: long molecule consisting of many similar or identical building blocks linked by covalent bonds, Polypeptide: polymers of amino acids Primary structure: protein is a linked series of amino acids with a unique sequence Prosthetic group Protein: a biologically functional molecule that consists of one or more polypeptides, each folded and coiled into a specific three-dimensional structure Quaternary structure: the overall protein structure that results from the aggregation of...
View Full Document

This note was uploaded on 02/07/2012 for the course BS 161 taught by Professor Dr.willkopachik,dr.ronpatterson during the Fall '11 term at Michigan State University.

Page1 / 5

Study_Guide_3_Proteins - Study Guide 3 Proteins/structure...

This preview shows document pages 1 - 3. Sign up to view the full document.

View Full Document Right Arrow Icon
Ask a homework question - tutors are online