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22 views10 pagesBiochemistry
Biochemistry is the study of chemical processes and substances in living organisms, focusing on biomolecules like proteins and nucleic acids. It plays a crucial role in understanding life processes, disease mechanisms, drug development, and biotechnology applications. The document also discusses carbohydrates, proteins, amino acids, and the importance of pH in biochemical reactions.
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0% found this document useful (0 votes)
22 views10 pagesBiochemistry
Biochemistry is the study of chemical processes and substances in living organisms, focusing on biomolecules like proteins and nucleic acids. It plays a crucial role in understanding life processes, disease mechanisms, drug development, and biotechnology applications. The document also discusses carbohydrates, proteins, amino acids, and the importance of pH in biochemical reactions.
Uploaded by
haiderali135797Copyright
© © All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
Available Formats
Download as PDF or read online on Scribd
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Definition: “ Biochemishy is the branch of science Khal explores
the — chemical processes and substances curing
within living organisms
> 4k focuses on the struclure Function, ond interoctions of
biewelecales, such os protems nucleic. acidr, catbohydales, and bpids
fo understand the mabculor mechanisms underlying Fe processes
is bi is try:
y Understonding Lfe processes: Biochamisty enplores chemical
processes within” Living organism, providing insights into fundamental
le furckon:
2) Molecular basis of disease: Clinical biochemistry play 0
crikical in pakient care by providing o valuable information for
Khe diagnosis, monitoring. and breatment of disease
3) Drug discovery and development: 46 lays o key re in
identiying and designing dug by studying the biochemical
pathway and interaction within the body.
u) Biotechnology and Genetic engeering: Bicchemisty 1s the
fundomental in manipulating DNA, leading to Gdvancement in
Voioledmology and gendlic engdasing for application in medicine,
agscalkue and industy.
5) Nubsilion and metabolism: Biachamistry explains the
Lhe chemical processes involved in the breakdown of nubionty
suck a5 carbohydrales, prolein, and fad duving digestion
9 Biological Research: Biochemisty is important in studying
caltular and molecular cesses, advancing our knodedge of
fundamental trolegical mechanisms droles:
v'
{arbobydalcs: which conlain corhan hydrogen and oxygen in
which hydrogen and onyger orepresent in the same rato
as in woler (2¥).”
1 ion: Cobohydiates ore the most abundanl biomolecule on
Toith However they only made 17 body mass of human
monosaccharide will not act on L-monosaccharde. Mort monosocchouide
present in mommals belong to D-type- vos
3) Anomers: —
Definition: There ore kno isomers that differ in configuration arcund
the anomeric carbon alon” .
Example: The catboy atom of carbonyl compound which is carban no. jn
alddbyde and caxbon ho-Linkelone . The ype of names are called & ond
Banomes. An example is x-P-glucse and 8-O-glucese.
sUnlike enanbomers, cnomers axe nol minor images af eachother
* A special fem disterecisomersm is used for a & B types of D-glucase.
4 Epimers:
Definition: “These are tno fsomerr thal differ in eenfiguration asound
the specific carbon atom other then the carbon clon
: ef chiro) carbon” ;
Ewample: Clucos and Galadom dliffer from each ather by) the
position of OH group ad carbon no. 4. They ase also called
Carbon U epimers Optical isomerism: i
Definition: “The enantiomeric monosaccharide by their content
of — asymmetric carbon volate the plane polarized -
inko vight or left Se
Desdlroratatyy: The compound which volades the plane polaiized .~
Light into right are called deutioratatiy and are designated @) . °
+ The compound which rotates the plane polorized
Lght into lefk aie called, terorololy and ove designated CJ.
Example: The naturally occuring glucose is dextrorolotry and
Galactose is lewrokalry.
The ving structure monosaccharide may be similar to either
pyran or furan and accordingly the monosacharide is said to
corcur in pyranose or furanose form. .
» Protein:
Word study: Protein is derived Grom greek word. means "prima ov est”
Definition: “Picters oc cellular mociorelecule which ave made
up amino acid polymers”
Composition: Protein an mainly composed of cabon hydsogen ioxyger
rikragen, phosphows and also sulphur ele
Nbundont biomolecule: They ase the most abundant organic.
Compound in cal which makes SOx or more of the dy moss of alt
Drnino Acid: Proteins ave mode up of amino acid: Amino acd ave the
building block of protein. Thee ore. twenty different amino acid which
rakes protein, Amino add are bonded to cack other by peptide bond.
They ae soluble in water and ore insoulble in fat sdlvents te
Chlorofarrn , acetone %
Struclure of Amino acid: There are four groups attached to A-Acid
1) Amino group. : .
2) Carbonylic group.
3) Alkyl group,
4) Hydrogen group. Alkyl group — Regu barylie group
Nw, — C — Coon
\
Arnino group ee Hydvog en group
0 Acid
Ariro acid can acl both os an acid as well ac a base .
depending upon the medium in which they are- placed a
Due fo this properly they ase also known as amphoteric electrolytes,
armphdyles or 2wilter ion
zwvitler ion: The ion which has both positive and negative charge
ut overall cany neutral charge
+The behaviour of amino acid at different pil ois shonn below.
u 8 . H
\ wt ( ae l -
R—C—cooh 5 R—C—coo & 6 coo
i We : .
Nug Nu Nil
At pH below At isoelectric pl AL
pl above
Woalestie ol (Neutral) isoelechic pi
cor (anion)
Stwucture_of Protein:
) Primary structure: The protein which is made, up of single
cham of amino acid having linear structure.”
Example: 4nsutin
2),Seco t 2 A long running polypeptide chain tends
to kwisl of coil oround idsel{ in a special patlern. This coiled
skuckure is held together by hydrogen bond. They container-helin Corr
Example: < keratin o* B planted. shee
3) Testiony structure: he long polypeptide chain of proteins undergo
folding and cefolding and gira rise to a definile thee dimensional
gkvwckure Tig structure is called ferkioly structure
Euample: Ribonuclease. WY Quakemary structure: Qualemary protein structure refers to the
awangement of bwo or more polypeptide chain (subunilss into
a single functional protein complen
Example: Mgoglabin (oxygen stooge) and hemoglobin oxygen canier J
Types of protein»
4)Globulor protein: They ore spherical or round shaped. They are
soluble in water.
2) Fibrous protein: They are thread like strudure having Linear shape.
They are. inscluble in water.
Function of protein: 1S?
YProtection: They assist in protection by playing role os
antibodies. Antibodies provide humoral immunity by killing
foreign antigens
2) Re Inction: Some protein ack as chemical
Signaling molecule called hormones. Homenes are secieled by
endocrine cells that help te control or ragulote different bedy
function re growth, metobolisen development and VET OT ion
B)Structure forming: A protein thal maker hairs and aaile is
keratin. keratin is produced by epithelial cells which makes different
body structure ie hatanail
Ww in: Sona protein transfer substance inside and
outside of cell ve gated protein , channel getled polein & canier
prokein. Hemaglobin is also & kansport protein that coy cuygen
to cells. ification of Amin id:
Arnino acid are classified based upon the presence of Alkyl
9xOup. Thee ace four classes of amino acid which ove given belo.
1) Non-pdiar Aliphadic R-group:
1) Glycine (Gly/G) 5) Leucine (Leu/L}
2) Alonine (Alo/A) 8) Tsoleucine (Tle/ I)
3) Proline (Pro! P) 7) Methionine (Mel/M)
W Vating (Nal/W
2) Avomatic &- group:
4) Phenylolanine (Phe/F)
2) Tyrosine (Ty)
3) Tryptophan — (Trp/W)
3) Polay Uncharged B-group:
hy Seviene (Sex/5)
ay Thesonine (Thr T)
3) Cysteine (Cys/C)
4 Glutamine — (Clu/Q)
5) Aspaigine (Asn /N
4) Positively chorged R-group:
1) lysisine (Lys /k)
YHislotine CHis/H)
3) Atgonine — (Arg)
5) Negatively chorged R group:
4) Aspartate ( Asp/*D)
2) Glukamede (Glu! E) =“ pil is a scale thal measurs the scidily or alkalinity
of oO soludion. St is defined as the negative log
of the hydrogen ion concentration ia moles per Litre
+The pit scale ranges fiom Oto 14
Scale:
+ ph 0-6: Acidic (Higher concentration of II" ions).
+ pt Tt Neukal Lequat concentration of tI and Ol” ions)
+ pl TIM Basic or alkeatine (higher concentration of GH” ions).
M calculgtion: pti = -log(H'}
Whee WH} is the hydrogen ion concentration
pou:
Definition: © POH iso meosure of the concentration of
hydroxide ions in a sdution. St Is negative log
of the hydrowide ion concentrator in odes /(ibre”
OW_c: jon: por= -log low
where (OH) is the hydouide ion concentration
pl ond Pon Relotion:
Consider a