AMINO ACIDS Amino acids are zwitterionic forms strong ionic bonds at isoelectric point (pI) Solubilities of amino

no acids are at a minimum at pI !attice energ" is most e#ot$ermic at t$is point as t$e zwitterions e#perience t$e greatest ionic attraction %witterions $a&e $ig$ melting points due to strong ionic bonds
Classification of amino acids Type Nonpolar Example (R group) 'l"cine (()) Alanine ((C)*) Negatively charged Aspartic acid ((C)+COO)) Positively charged !"sine (((C)+),N)+) Uncharged Serine ((C)+O)) C"steine ((C)+S))

Reactions of amino acids -wo important reactions to remember Salt formation )*N.(/(COO( . ). )*N.(C)/(COO) )*N.(/(COO( . O)( )+N(C)/(COO( . )+O ydrolysis of peptides Acidic $"drol"sis ). 4 $eat (/(CON)(/1( (/(COO) . )*N.(/1(

0eptide bond formation )*N.(/(COO( . )*N.(/1(COO( )*N.(/(CON (/1(COO( . )+O peptide bond 3nz"matic $"drol"sis Ma" be catal"zed b" enz"mes li5e tr"psin4 pepsin etc

2asic $"drol"sis O)( 4 $eat /(CON)(/1 (/(COO( . )+N(/1(

0/O-3INS -$e primary structure of a protein refers to t$e number and se6uence of amino acids in a pol"peptide c$ain 3 g 7 ala(gl"(leu(t"r($is(ala(leu(p$e
-$e secondary structure of a protein refers to t$e local spatial conformation of t$e pol"peptide bac5bone4 in t$e form of eit$er 8($elices or 9(pleated s$eets 8($eli# 9(pleated s$eet /ig$t($and screw Stabilized b" $"drogen(bonds between CO and N) groups in ad;acent strands N) group in eac$ peptide lin5 is $"drogen(bonded to t$e CO group of t$e Ma" be antiparallel or parallel fourt$ following peptide lin5 Side c$ains on successi&e AA residues * : AAs per turn appear on opposite sides of t$e s$eet -$e tertiary structure of a protein refers to its t$ree(dimensional structure of t$e pol"peptide < )"drogen bonding a 2etween polar side c$ains ((O)4 (N)4 =O4 =N/ groups) + &an der >aals forces a 3lectrostatic interactions among permanent or induced dipoles b )"drop$obic interactions contributed b" nonpolar side c$ains w$ic$ cluster awa" from water to a&oid destabilisation of side c$ains (a $"drop$obic core is formed) * Ionic interactions a 2etween two oppositel" c$arged side c$ains (e g Asp and !"s) usuall" groups t$at ionize in water , Disulp$ide bridges a 2etween c"steine residues wit$ t$e t$iol ((S)) side c$ain b /(S) . )S(/1 . ?O@ /(S(S(/ . )+O -$e !uaternary structure of protein refers to t$e spatial arrangements and association of t$e pol"peptide subunits of proteins )aemoglobin as an e#ample o Aormed from four pol"peptide c$ains

D3NA-B/A-ION OA 0/O-3INS "enaturation refers to t$e disruption in t$e secondar"4 tertiar" and 6uaternar" structure of proteins b" t$e brea5ing of t$e non(co&alent (but including disulp$ide bridges) interactions t$at $old t$ese structures in t$eir nati&e conformation
Effect of Temperature )eating causes an increase in t$e t$ermal &ibration of t$e molecule )"drogen bonding is disrupted 0roteins denature and t$us unfold Effect of p If p) is lowered far below pI4 t$e protein will onl" contain positi&e c$arges !i5e c$arges repel eac$ ot$er and cause t$e denaturation of proteins !i5ewise for $ig$ p) Effect of eavy #etal $ons )ea&" metal ions (0b+.4 Cd+.4 etc) are positi&el" c$arged Compete wit$ positi&el" c$arged groups for attraction wit$ negati&el" c$arged groups Also bond wit$ S) groups (especiall" )g+.) and disrupt disulp$ide bridges /esident metal ions in certain proteins ma" also be displaced

3 N % CM 3 S 3nz"mes are biological catal"sts t$e" increase t$e rate of reaction wit$out t$emsel&es being c$anged at t$e en d of t$e reaction -$e" catal"ze reactions b" pro&iding an alternate route of reaction wit$ lower acti&ation energies
Characteristics Specificit"7 onl" certain substrates are acted upon b" enz"mes4 and onl" a single t"pe of reaction ta5es place !arge catal"tic power7 some enz"mes can speed up reactions b" a billion times