Nature of lectin carbohydrate interactions and how to treat
them by computational chemistry tools

D 2009

Nature of lectin carbohydrate interactions and how to treat them by computational chemistry tools

MISHRA, Sushil Kumar; Jan ADAM; Zdeněk KŘÍŽ; Michaela WIMMEROVÁ; Jaroslav KOČA et al.

Základní údaje

Originální název

Nature of lectin carbohydrate interactions and how to treat them by computational chemistry tools

Název česky

Povaha lektin sacharidových interakcí a jejich zkoumání pomocí výpočetní chemie

Autoři

MISHRA, Sushil Kumar; Jan ADAM; Zdeněk KŘÍŽ; Michaela WIMMEROVÁ a Jaroslav KOČA

Vydání

Netherlands, Glycoconjugate Journal, "20th International Symposium on Glycoconjugates Glycans: From Molecules to Structures to Therapeutics, San Juan, Puerto Rico. od s. 875-876, 1 s. 2009

Nakladatel

Springer

Další údaje

Jazyk

angličtina

Typ výsledku

Stať ve sborníku

Obor

10403 Physical chemistry

Stát vydavatele

Česká republika

Utajení

není předmětem státního či obchodního tajemství

Impakt faktor

Impact factor: 2.500

Označené pro přenos do RIV

Organizační jednotka

Přírodovědecká fakulta

ISSN

Klíčová slova česky

lectin engineering; molecular modeling; thermodynamics

Klíčová slova anglicky

lectin engineering; molecular modeling; thermodynamics

Změněno: 8. 4. 2010 13:56, Ing. et Ing. Jan Adam, Ph.D.

Anotace

ORIG CZ

V originále

Recognition in biological systems is often mediated through protein/carbohydrate interactions. Proteins that bind carbohydrates are called lectins. As the number of combinations that may create the saccharide code is extremely large, lectins must be very carefully designed by Nature to read and decipher such a complicated alphabet. The key role during the process of such deciphering is played by protein/carbohydrate interaction energy. The forces that keep lectin/carbohydrate complexes together are based either on polar interactions between the polar carbohydrate groups, represented especially by oxygen atoms, and polar protein functional groups. This kind of interactions may often be mediated or enlarged by bridging water molecules, or by ions. The last option usually generates strong interactions leading to stable lectin/carbohydrate complexes.

Česky

Prace se zabyva povahou lektin-sacharidovycm interakci v ruznych zkoumanych systemech, rozdilem povahy elektrostatickych polarnich versus hydrofobnich interakci, a zpusoby, jakymi je mozno k temto interakcim pristupovat z pohledu molekuloveho modelovani.

Návaznosti

LC06030, projekt VaV

Název: Biomolekulární centrum

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, Biomolekulární centrum

Citovat

MISHRA, Sushil Kumar; Jan ADAM; Zdeněk KŘÍŽ; Michaela WIMMEROVÁ a Jaroslav KOČA. Nature of lectin carbohydrate interactions and how to treat them by computational chemistry tools. In Glycoconjugate Journal, "20th International Symposium on Glycoconjugates Glycans: From Molecules to Structures to Therapeutics, San Juan, Puerto Rico. Netherlands: Springer, 2009, s. 875-876, 1 s. ISSN 0282-0080.

@inproceedings{863898,
   author = {Mishra, Sushil Kumar and Adam, Jan and Kříž, Zdeněk and Wimmerová, Michaela and Koča, Jaroslav},
   address = {Netherlands},
   booktitle = {Glycoconjugate Journal, "20th International Symposium on Glycoconjugates Glycans: From Molecules to Structures to Therapeutics, San Juan, Puerto Rico.},
   keywords = {lectin engineering; molecular modeling; thermodynamics},
   language = {eng},
   location = {Netherlands},
   pages = {875-876},
   publisher = {Springer},
   title = {Nature of lectin carbohydrate interactions and how to treat them by computational chemistry tools},
   year = {2009}
}

TY  - CONF
ID  - 863898
AU  - Mishra, Sushil Kumar - Adam, Jan - Kříž, Zdeněk - Wimmerová, Michaela - Koča, Jaroslav
PY  - 2009
TI  - Nature of lectin carbohydrate interactions and how to treat them by computational chemistry tools
PB  - Springer
CY  - Netherlands
KW  - lectin engineering
KW  - molecular modeling
KW  - thermodynamics
N2  - Recognition in biological systems is often mediated through protein/carbohydrate interactions. Proteins that bind carbohydrates are called lectins. As the number of combinations that may create the saccharide code is extremely large, lectins must be very carefully designed by Nature to read and decipher such a complicated alphabet. The key role during the process of such deciphering is played by protein/carbohydrate interaction energy. The forces that keep lectin/carbohydrate complexes together are based either on polar interactions between the polar carbohydrate groups, represented especially by oxygen atoms, and polar protein functional groups. This kind of interactions may often be mediated or enlarged by bridging water molecules, or by ions. The last option usually generates strong interactions leading to stable lectin/carbohydrate complexes.
ER  -

MISHRA, Sushil Kumar; Jan ADAM; Zdeněk KŘÍŽ; Michaela WIMMEROVÁ a Jaroslav KOČA. Nature of lectin carbohydrate interactions and how to treat them by computational chemistry tools. In \textit{Glycoconjugate Journal, ''20th International Symposium on Glycoconjugates Glycans: From Molecules to Structures to Therapeutics, San Juan, Puerto Rico.}. Netherlands: Springer, 2009, s.~875-876, 1 s. ISSN~0282-0080.

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