Biochemistry 2280A Study Guide - Midterm Guide: Sumo Protein, Covalent Bond, Lipoprotein
30 Apr 2018
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Biochemistry 2280 – Midterm
Protein Domain
Be able to describe a protein doais characteristics
▪ distinct region of a protein (sequence of amino acids)
▪ independently folded
▪ provide structure and/or function
▪ may have many or only one
▪ related domains are found in different proteins (evolution)
Learn how proteins fold and how they become unfolded
- folding pathways are likely specified by primary sequence
- thousands of weak interactions
- molecular chaperones; proteins that help with folding
- stepwise process; hydrophobic interactions, then secondary, then tertiary
- a folded, biologically active protein is considered to be in its atural
state (least free energy)
- can be denatured — then have random, flexible conformation activity
• because of exposed hydrophobic groups, they aggregate and
precipitate (like frying an egg)
• when denaturing condition is removed, some will refold
(renaturation)
• some proteins have difficulty renaturing — need molecular chaperons
Understand the concept of protein families
- related by evolution
- new families come from old ones
- similar protein sequence, structures, functions and domains
- many proteins combine tightly with other substances such as carbohydrates gloproteis,
lipids lipoproteis or metal ions etalloproteis
- proteins derived from the same ancestor are called hoologous proteis
- can give clue to structure and function of protein
- residues critical for function dot change with evolution; oserved residues (ex. steroid
receptors)
Be able to list different functions of proteins
Enzyme — catalyzes covalent bond breakage or formation
Structural — provides mechanical support to cells and tissues
Transport — carries small molecules or ions
Motor — generates movement in cells and tissues
find more resources at oneclass.com
find more resources at oneclass.com
Document Summary
Be able to describe a protein do(cid:373)ai(cid:374)(cid:859)s characteristics: distinct region of a protein (sequence of amino acids, independently folded, provide structure and/or function, may have many or only one, related domains are found in different proteins (evolution) Learn how proteins fold and how they become unfolded. Folding pathways are likely specified by primary sequence. Molecular chaperones; proteins that help with folding. Stepwise process; hydrophobic interactions, then secondary, then tertiary. A folded, biologically active protein is considered to be in its (cid:858)(cid:374)atural state(cid:859) (least free energy) Similar protein sequence, structures, functions and domains. Many proteins combine tightly with other substances such as carbohydrates (cid:894)(cid:858)gl(cid:455)(cid:272)oprotei(cid:374)s(cid:859)(cid:895), lipids (cid:894)(cid:858)lipoprotei(cid:374)s(cid:859)(cid:895) or metal ions (cid:894)(cid:858)(cid:373)etalloprotei(cid:374)s(cid:859)(cid:895) Proteins derived from the same ancestor are called (cid:858)ho(cid:373)ologous protei(cid:374)s(cid:859) Can give clue to structure and function of protein. Residues critical for function do(cid:374)(cid:859)t change with evolution; (cid:862)(cid:272)o(cid:374)served residues(cid:863) (ex. steroid receptors) Be able to list different functions of proteins. Enzyme catalyzes covalent bond breakage or formation.
