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UMD / Biology / BIOL 103 / Where are hydrogen bonds found?

Where are hydrogen bonds found?

Where are hydrogen bonds found?

Description

School: University of Minnesota Duluth
Department: Biology
Course: Evolution
Term: Fall 2016
Tags: Bonding, regulation, protein, DNA, RNA, transcription, translation, tRNA, mRNA, condensation, hydrolysis, hydrogen, structure, Enzyme, Lysozyme, Inhibition, feedback systems, covalent, euchromatin, heterochromatin, histone, nucleosome, ribose, deoxyribose, RNApolymerase, Codon, anti-codon, ribosomes, eukaryotes, prokaryotes, and Genome
Cost: 50
Name: Exam 1 Cell Biology Study Guide
Description: Condensed notes from chapters 1, 2, 4, 5, and 7 for Exam 1
Uploaded: 09/18/2016
10 Pages 50 Views 3 Unlocks
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Exam 1 STUDY Guide


Where are hydrogen bonds found?



Cell Bio

ads

are between

it

+ O or N

possible

como combos

H-N-R

H-O-R

ÖR

ÖR

H-O-R

N=R

H -N-R

WAR

Building blocks

sugats -

fatty acids Amino acids > nucleotides →


What does condensation do to water?



in plants a larger organic mdeales o polysaccharides, glycogen, & Starch

falts fats & membrane lipids proteins nucleic acids

what is a condensation to Hydrolysis cxn?

condensation removes H2O

R-OH + HR

- R-R + H2O

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Which bonds are weak in aquaeous solution?



Hydrolysis rans use tho to break a boadi Ex wl aa's e Re If you want to learn more check out What comprises a community?

H2N-C-C-N-C-COOH + H2g

J-7

Z-I

o-I

H Don't forget about the age old question of How do we recognize the style of an object?

Ri

H2N-C-Coll

+

(HEN-C-COOH

• What forces determine the folding shape

of a macromoleccle ?

noncovalent bonds between the subunits

of a macromolecule

Ex ionic bonds, t-bonds of van derwaals,

& hydrophobic interactions (covalent bonds link the polypeptide string

together) If you want to learn more check out Who came up with pasteurization?

Remember that noncoralenta c. weak in aqueous soln

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proteins by heating

can easily be unfolded the soln

Dadi

Also, the shape of a protein is specified by the AA sequence

I proteins fold into a conformation of lowest energy I structure linear sequence

backbone H-bonding

& helices & & sheets H-bonding, ionic, covalent,

Van der waal Can have backline + R-group banding : multiple subunit noncovalent If you want to learn more check out What is bioremeditation?
Don't forget about the age old question of How much of our body is made up of water?

bonds a helices The R-groups stick outwards.

H bonds between the backbone atoms stabilize a helices

vaals,

• B Sheet H bonds are formed

the backbone atoms

between not

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a helizes

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There is no R-group bonding in B shelts The R-groups extend above & below the plane of the ß sheet, Don't forget about the age old question of What are the general routes for pathogens to enter the body?

y This could result in 2 totally different chemical environments (the

top above the ß sheet & below it,

Acidic a R-groups cold poke up above the & sheet while below it hydropobic r groups polce din.

o chaperone proteins

even though on their own

help

proteins

proteins fold up,

can fold up

Lysozyme - catalyzes hydrolysis to

a break a part polysaccharides in the cell walls of bacteria

Glutamic acid Aspartic acid help the run in the activesite

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10oP

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• Protein regulation

Feedback inhiblica e an enzyme is either inhibited or stimulated by its product

o positive feedback loop feedback loop "negative regulation" "positive requanin!

negative

Conformational changes whether a substrate

active site or not

of enzymes influence

can hit in the

upy

phosphorylation can cause a confermananal change either activating or deactivating

I an enzyme The phosphate group comes from an ATP moeccle (the terminal Phosphate

grap) catalyzed by protein kinase The reverse rxn is done by

protein phosphatase Other covalent modifications, that can change

the shape of an enzyme /protein: --acetylation

- attachment of Ubiquitin.

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DNA

RNA

-pzo

o-p=0

Inbase

N base

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Op=o

Olt

olt

- double stranded - ATGC

- singlestrandled usually

- (can be double

Stranded) - AU G C

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• genomeno correlation between

T the size of an organism's genome & the complexity of I organism

the

Histones

histure

octamer

8 histone proteins

2x z

H2A H 2 B H3 HY

vally

- 147 nucleotides of dabe stranded

DNA wraps around a histone

( 1.7 times around). - The linker DNA can vary in length

Histones are 0 charged

DNA is one each Histone protein in the octamer has a long terminus tail

that stickas out. Conformation changes of this tail regulates the chromatin

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expressed DNA most likely is

kept as euchromatin unexpressed ONA > Heterochromatin

STUDIO

o Transcription

5

RNA polymerase reads the template strand 3 5 ' and synthesises

the new RNA strand 5 31 5' is capped w/ a methylated

Guanine & the 3 end is poly adenylated

Introns are also spliced out before mRNA can be exported from the nucles.

also make

The post TX modifications the mRNA more stable

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Translation

ng

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codon → 3 nucleotides on warna anticodon on the tRNA translation is 5'-3

a nbosome begins translation when the Met tRNA in the posite of the ribosome identities the start codon

AUG. ERNAS come in starting @ the

A site of the nbosone, moving to the P-site & then Este as the nbosome translocates down the mRNA transcript

late

ER PCA

uis

- in proks , there is no nucleus so

translation can start immediatley, after even if the mRNA is still being transcribed.

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- a lot of

several translated

prok mRNAS code for proteins that can be

from the same mRNA

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