📘 ❞ Chaperonin Protocols ❝ كتاب ــ Christine Schneider اصدار 2010
Biology Books - 📖 ❞ كتاب Chaperonin Protocols ❝ ــ Christine Schneider 📖
█ _ Christine Schneider 2010 حصريا كتاب Chaperonin Protocols 2024 Protocols: نبذه عن الكتاب: Purification of Archaeal Chaperonin from Sulfolobus shibatae Elsie Quaite Randall and Andrzej Joachimiak 1 Introduction Sulfolobus shibatae is a hyperthermophilic archaeon that was first identified living in acidic geothermal hot springs This organism grows optimally at pH 3 0–4 0 83°C (1), however it over the temperature range 75– 85°C When S subjected to higher temperatures (85–90°C) heatshock response observed major protein induced large ring structure TF55 (2), also called archaeosome (3) or rosettasome (4), which is composed two different subunits designated ` (3,4) Apart from the presence subunits, another difference between this molecule the prokaryotic GroEL number per ring In shibatae, nine subunits form each compared with seven The similarity double (2,3) GroEL, together the fact were 60 kDa, heat shock protein, was active folding, suggested archaeal chaperonin (2) and was similar function However, comparison primary structure showed both more closely related TCP 1 family of polypeptides, eukaryotic cytosolic (2,4,5) contrast the archaeal chaperonin, comprises eight sequence characteristic “double doughnut ” The therefore gives us simplified version of the by may be possible determine characteristics mammalian cytoplasmic chaperonins are often referred as Type II chaperonins from S (6) related, sequence Biology Books مجاناً PDF اونلاين Biologically Biology natural science concerned study life, its various forms function, how these organisms interact other surrounding environment word biology Greek made up words: bio (βίος) meaning life And loggia ( λογία) means Biology: vegetation animal cover on edges African American states, existence same fossil Branches biology Biology an ancient thousands years old modern began nineteenth century has multiple branches Among them are: Anatomy Botany Biochemia Biogeography Biofisia Cytology cell science Ecology environmental science Development Embryology embryology Genetics genetics Histology histology Anthropology anthropology Microbiology bacteriology Molecular Biology Physiology functions organs Taxonemia taxonomy Virology virology Zoology zoology
كتاب
Chaperonin Protocols
ــ Christine Schneider
صدر 2010م
كتاب
Chaperonin Protocols
ــ Christine Schneider
صدر 2010منبذه عن الكتاب:
Purification of Archaeal Chaperonin
from Sulfolobus shibatae
Elsie Quaite-Randall and Andrzej Joachimiak
1. Introduction
Sulfolobus shibatae is a hyperthermophilic archaeon that was first identified
living in acidic geothermal hot springs. This organism grows optimally at pH
3.0–4.0 and 83°C (1), however it grows over the temperature range of 75–
85°C. When S. shibatae is subjected to higher temperatures (85–90°C) a heatshock response is observed and the major protein induced is a large ring
structure TF55 (2), also called archaeosome (3) or rosettasome (4), which is
composed of two different subunits (4), designated _ and ` (3,4). Apart from
the presence of two subunits, another difference between this molecule and the
prokaryotic GroEL is the number of subunits per ring. In S. shibatae, nine
subunits form each ring compared with seven in GroEL.
The similarity of this double ring (2,3) to that of GroEL, together with the
fact that the subunits were 60 kDa, it was a heat-shock protein, and it was
active in protein folding, suggested that it was the archaeal chaperonin (2) and
was similar in function to GroEL. However, comparison of the primary structure showed that both subunits were more closely related to the TCP-1 family
of polypeptides, the eukaryotic cytosolic chaperonin (2,4,5). In contrast to the
archaeal chaperonin, the eukaryotic cytosolic chaperonin comprises eight
sequence-related polypeptides, which also form the characteristic “double
doughnut.” The archaeal chaperonin therefore gives us a simplified version of
the eukaryotic chaperonin by which it may be possible to determine characteristics of the eukaryotic chaperonin. Archaeal and mammalian cytoplasmic
chaperonins are often referred to as Type II chaperonins. The chaperonin from
S. shibatae is a Type II chaperonin (6) and is related, by primary sequence
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