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Proteins: primary and secondary structure (Czech)
From Proteopedia
(Difference between revisions)
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*'''Sekundární struktura'''- Ve většině proteinů se nachází dva typy sekundární struktury. | *'''Sekundární struktura'''- Ve většině proteinů se nachází dva typy sekundární struktury. | ||
| - | :*<scene name='60/603296/Secundaria/4'>Alfa-helix</scene>– spirálovitá struktura s výškou závitu 0,56 nm s <scene name='60/603296/Secundaria/5'>kruhovým | + | :*<scene name='60/603296/Secundaria/4'>Alfa-helix</scene>– spirálovitá struktura s výškou závitu 0,56 nm s <scene name='60/603296/Secundaria/5'>kruhovým vnitřním průřezem</scene>. Nyní <scene name='60/603296/Secundaria/7'>skryjeme vodíky</scene>. Kostra polypeptidového řetězce tvoří spirálu na vnitřním okraji struktury a postranní řetězce jednotlivých aminokyselin vyčnívají ven do prostoru. Nyní skryjeme postranní řetězce pro přehlednější zobrazení <scene name='60/603296/Secundaria/8'>od konce</scene> a <scene name='60/603296/Secundaria/10'>ze strany</scene>. Takzvaný <scene name='60/603296/Secundaria/11'>ribbon model</scene> zvýrazňuje spirálovitou strukturu hlavního řetězce, zatímco <scene name='60/603296/Secundaria/13'>atomární model</scene> ukazuje uspořádání postranních řetězců. ''Alfa-helix''je struktura zpevněná mnoha <scene name='60/603296/Secundaria/14'>vodíkovými můstky</scene>. Každá skupina tvořící peptidovou vazbu tvoří vodíkové můstky se skupinami v okolních smyčkách spirály. |
:*Primary structure specifies secondary structure, i.e., is the amino acid sequence which determines that a polypeptide chain folds resulting a alfa helix or other secondary structure. Let's consider the effects of <scene name='60/603296/Secundaria/20'>electrical charged residues</scene> of either sign and the <scene name='60/603296/Secundaria/21'>side chains size</scene>. | :*Primary structure specifies secondary structure, i.e., is the amino acid sequence which determines that a polypeptide chain folds resulting a alfa helix or other secondary structure. Let's consider the effects of <scene name='60/603296/Secundaria/20'>electrical charged residues</scene> of either sign and the <scene name='60/603296/Secundaria/21'>side chains size</scene>. | ||
:*'''<scene name='60/603296/Secundaria2/1'>Beta sheet</scene>'''.- Polypeptide chain is folded in zigzag arrangement. Let's <scene name='60/603296/Secundaria2/2'>hide hydrogen atoms</scene> and <scene name='60/603296/Secundaria2/3'>side chains</scene> for a better understanding. Notice that a polypeptide chain can have several linear fragments separated by curvatures called ''beta turns''. Now let's recover <scene name='60/603296/Secundaria2/4'>side chains</scene> and highlight the <scene name='60/603296/Secundaria2/5'>hydrogen bonds</scene> between different linear sections of the chain. This hydrogen bonds give stability to the structure. Let's look now the polypeptide chain represented by a <scene name='60/603296/Secundaria2/6'>ribbon model</scene>. | :*'''<scene name='60/603296/Secundaria2/1'>Beta sheet</scene>'''.- Polypeptide chain is folded in zigzag arrangement. Let's <scene name='60/603296/Secundaria2/2'>hide hydrogen atoms</scene> and <scene name='60/603296/Secundaria2/3'>side chains</scene> for a better understanding. Notice that a polypeptide chain can have several linear fragments separated by curvatures called ''beta turns''. Now let's recover <scene name='60/603296/Secundaria2/4'>side chains</scene> and highlight the <scene name='60/603296/Secundaria2/5'>hydrogen bonds</scene> between different linear sections of the chain. This hydrogen bonds give stability to the structure. Let's look now the polypeptide chain represented by a <scene name='60/603296/Secundaria2/6'>ribbon model</scene>. | ||
Revision as of 21:32, 26 February 2019
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