AndMotioninBiology



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2.2 SecondaryStructure


Thesecondarystructureistheinitialfoldingoftheaminoacidsequenceintoalphahelicesandbetasheets(Figure2).


Theaminoacidsinanalphahelixarearrangedinahelicalstructureabout5angstromsindiameter.Eachaminoacidresultsina100degreeturninthehelix;thusthereare
3.6aminoacidsperturn.AsshowninFigure2,theRsidechainsarelocatedontheexteriorofthehelix.Hydrogenbonds(indicatedbythedottedlines)formbetweenthe
Figure2:Secondarystructures:a.alphahelix;b.betasheet

Figure3:Threetypesofbetasheets


N-H group of one amino acid and the C=O group of an amino acid four spaces awaybecausethesetwoaminoacidsarelocatedalmostdirectlyontopofoneanotherduetothe 3.6 amino acids per turn of the helix. These hydrogen bonds help stabilize the alphahelixstructure.


The beta sheet consists of a series of adjacent and parallel strands of the same proteinarrangedinasheet-likeform.HydrogenbondsformbetweentheN-Hgroupsofonestrandand the C=O groups of an adjacent strand.Beta sheets can be antiparallel, parallel, ormixed (Figure 3).In antiparallel form, the strands have alternating orientation and thehydrogenbondsareperpendiculartothestrands.Inparallelform,thestrandsallhavethe same orientation and the hydrogen bonds are at angles to the strands. This form ismuch less common than the antiparallel form. In addition, a beta sheet can be a mixtureofparallelandantiparallelsections.OftenbetasheetsfoldsuchthatthehydrophobicR side chains are on one side of the sheet and the hydrophilic R side chains are on theotherside.
Figure4:Ribbonrepresentationoftertiarystructure


    1. 2.3.Tertiary Structure


Thetertiarystructureofaproteinisthearrangementofsecondarystructureelementsto form an overall three-dimensional structure (Figure 4).These tertiary structures aregenerally compact with hydrophilic side chains on the outer surface and the hydrophobicside chains buried in the interior. As in the secondary structure, hydrogen bonds help tostabilize the tertiary structure in its major conformation. In addition, cysteine bridgesmay form through disulfide bonds between cysteine amino acids (see special amino acidsFigure1).Thesecovalentbondshelpfurtherstabilizetheprotein.



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