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Cellular and Molecular Biology Lecture 4

Terms in this set (20)

More than 50% of the dry weight of cells is p________.
protein
Proteins have comp_____ and uni_____ __-__ struc_______s
complex, unique 3-D structures
All amino acids have an al_____ ca______, a car______ gr_____ and an am_____ gr______. The si____ ch_____ or __ gr_____ is dif_____ in each amino acid and these side chains dictate how the amino acid will beh_____.
alpha carbon, carboxyl group, amino group, side chain, R group, different, behave
The 3 types of amino acids (based on proper_____s of their __ g_____s):
no__-p______ - hydr_________
po_____ - hydrop________
elec________y ch_________d - hydrop_________
properties, R groups, non-polar, hydrophobic, polar, hydrophilic, electrically charged, hydrophilic
Peptide bonds link the carb_____ gr____ of one am____ ac______ to the ami____ gr_____ of the next. This is a deh_______ re_______, forming __________. As the polypeptide is built, there is a repe_______e bac_______. The folding of the polypeptide is dictated by the sequ_____ of si____ ch______s.
carboxyl group, amino acid, amino group, dehydration reaction, water, repetitive backbone, sequence, side chains
The primary structure of proteins is the seq______ of the ami____ ac____s in a whole pol_____________e.
sequence, amino acids, polypeptide
An amino acid sequence in a polypeptide is specified by the seq______ of nucl________s in __ __ __. This information is copied into __ __ __ __. The information in the mRNA is tran________d into a spec______ am____ ac_____ seq_________.
sequence, nucleotides, DNA, mRNA, translated, specific amino acid sequence
The secondary structure of proteins can be either an al____ he_____ or a b____ pl______ sh______. These secondary structures are stabil______d by the presence of hyd______ b______s between the b_________ of the amino acid chain. Hydrogen bonds are normally quite w____, however, because there are so many of them, it is enough for stab_________n of the secondary structures. R groups can interfere with the fo_______ of hydro_____ bo____s by their si___ and ch_____. This is ster_____ hind________e.
alpha helix, beta pleated sheet, stabilised, hydrogen bonds, backbone, weak, stabilisation, formation, hydrogen bonds, size, charge, steric hindrance
An alpha helix is a deli_____ co____ held together by __________ b_______g between every f_____h ami____ ac___. They are usually found in tra____________ pro_______s that cross the li_____ bil________.
delicate coil, hydrogen bonding, fourth amino acid, transmembrane proteins, lipid bilayer
Each beta strand in a beta pleated sheet is shown as alternating fl____ ar______s. There are h_________ b_____s between each beta str_____. It is essentially t___ or mo____ str______s of the same poly________ ch______ laying si___ b__ s____. H________ b______s form between O and H of nei________g pol________ backb________s. Beta pleated sheets often make up the c_____ of many glo______ pr_______s
flat arrows, hydrogen bonds, strand, two, more strands, polypeptide chain, side by side, hydrogen bonds, neighbouring polypeptide backbones, core, globular proteins
Spider silk is made of b____ pl_____ sh______s
beta pleated sheets
The tertiary structure of proteins describes the over_____ __-__ confo_________ of the p___________ ch_______. It is stabalised by int___________s between si____ ch_____s. These interactions include hyd______ b_____s between si____ ch______s, hydr_______c interactions and v___ d___ w______s in_________s, i____c b_____s and disu______ br_______s. These are all relatively w____ interactions except the dis______ b_______s which are str_____ cov_____ b_____s
overall 3-D conformation, polypeptide chain, interactions, side chains, hydrogen bonds, side chains, hydrophobic, van der waals interactions, ionic bonds, disulfide bridges, weak, disulfide bridges, strong covalent bonds
The quaternary structure is the fin___ str_______ formed when a protein consists of t___ or m____ pol___________s. These polypeptides can be the s____ or d_______. The polypeptides are held together by intera_______s between a_____ a____ si____ ch_____s.
final structure, two, more polypeptides, same, different, interactions, amino acid side chains
Quaternary Structure :
-collagen consists of 3 id______ pol____________s which intertw______, forming a str____ collagen fi____.
-Hem______ in the bl____ is also a qua_______ pr______.
identical polypeptides, intertwine, strong fibre, hemoglobin, blood, quaternary protein
Chaperonins assist in the fo_____g of p_______s. They do this by protecting the poly_________ from degr_________n and also by providing the id____ env_______ for polyp______s to fo____ spon_______________y into pr_______s. A chaperonin consists of a c___ and a hol____ cyl______. Some chaperonins, together with ass_______d sys______s check correct fol____g has occ______d. If an misfold has occurred they can help with refo_____g or mark it for dest________.
folding, proteins, polypeptide, degradation, ideal environment, polypeptides, fold spontaneously, proteins, cap, hollow cylinder, associated systems, folding, occurred, refolding, destruction
A chaperonin consists of ____ pro_____s: a c___ and a ho_____ cy______. The cap op____s and an unfo______ pol___________ enters the cy_______ from one end. The cap then att______s, causing the cyli______ to cha___ sh____ such that it creates a hydr_______ env__________ for the fol_____g of the pol__________. The c___ then comes off and the properly fo_____d pro____ is re_______d.
two proteins, cap, hollow cylinder, opens, unfolded polypeptide, cylinder, attaches, cylinder, change shape, hydrophilic environment, folding, polypeptide, cap, folded protein, released
The denaturation of a protein refers to the loss of its __-__ st________. This means the destr______ of the se______, ter_____ and qu________ structures and we are left with only the pr______ st______. This means the bre_____g of h______ b_____s, hydrophilic and hy_______ inter________s and S=S b____s.
3-D structure, destruction, secondary, tertiary, quaternary, primary structure, breaking, hydrogen bonds, hydrophobic interactions, bonds
Denaturation of a Protein can be caused by:
-He____ which breaks w___ b___s
-__ __ which changes ionis_____ patt_____s of __ gr_____s
-Red_____g ag_____s which reduce dis______ bri______s to SH.
-Orga_____ solv______s which disturb hydropho_____ and hy_______ inter_______s
-Deter_______s which disrupt hydr_________ in__________s.
heat, weak bonds, pH, ionisation patterns, R groups, reducing agents, disulfide bridges, organic solvents, hydrophobic, hydrophilic interactions, detergents, hydrophobic interactions
Hydrolysis of a polypeptide involves adding a mo_____ of w______ which breaks a pep_____ b_____.
molecule, water, peptide bond
Some denatured proteins can ret____ to their func______l sh_____ if the den_______g ag_____ is rem_______d
return, functional shape, denaturing agent, removed
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