𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Genetic and biochemical analysis of in vivo protein folding and subunit assembly

✍ Scribed by David P. Goldenberg; Donna H. Smith; Jonathan King

Publisher
Wiley (John Wiley & Sons)
Year
1983
Tongue
English
Weight
273 KB
Volume
22
Category
Article
ISSN
0006-3525

No coin nor oath required. For personal study only.

✦ Synopsis

The in uiuo pathway of folding and subunit assembly of a trimeric bacteriophage protein has been studied by characterizing precursors to the native protein and by analyzing temperature-sensitive mutations that kinetically block the pathway. The native trimer is formed via an intermediate composed of three partially folded chains, the protrimer. At 39"C, temperature-sensitive mutations prevent the formation of both the native trimer and the protrimer, possibly by destabilizing earlier intermediates. However, the mutations do not affect the stability of the native protein, formed a t 30Β°C. Thus, these mutations identify amino acid residues involved in interactions that determine the folding pathway.

πŸ“œ SIMILAR VOLUMES

Assembly of the QM protein onto the 60S
Assembly of the QM protein onto the 60S ribosomal subunit occurs in the cytoplasm
✍ Yen H. Nguyen; Alea A. Mills; Eric J. Stanbridge πŸ“‚ Article πŸ“… 1998 πŸ› John Wiley and Sons 🌐 English βš– 153 KB

QM is a human cDNA originally isolated as a transcript elevated in a nontumorigenic Wilms' tumor microcell hybrid, relative to the tumorigenic parental cell line. The QM gene encodes a 24 kDa basic protein that peripherally associates with the ribosomes. Recently, the gene for this protein has also

Cloning and expression analysis of a G-p
Cloning and expression analysis of a G-protein subunitβ€” in the rice water weevil lissorhoptrus oryzophilus Kuschel
✍ Gui-Juan Kang; Zhong-Jun Gong; Jia-An Cheng; Cun-Gui Mao; Zeng-Rong Zhu πŸ“‚ Article πŸ“… 2010 πŸ› John Wiley and Sons 🌐 English βš– 271 KB

The open reading frame (ORF) encoding a novel G protein a subunit, Lo Ga o , was cloned from the parthenogenetic rice water weevil, Lissorhoptrus oryzophilus Kuschel (Coleoptera: Curculionidae). The Lo Ga o ORF encodes a protein of 354 amino acid residues. The deduced protein sequence shares high ho

Glycogen storage disease type II: Geneti
Glycogen storage disease type II: Genetic and biochemical analysis of novel mutations in infantile patients from Turkish ancestry
✍ Monique M. P. Hermans; Marian A. Kroos; Jan A. M. Smeitink; Ans T. van der Ploeg πŸ“‚ Article πŸ“… 1998 πŸ› John Wiley and Sons 🌐 English βš– 192 KB πŸ‘ 1 views

Glycogen Storage Disease type II (GSDII) is caused by the deficiency of lysosomal a-glucosidase (acid maltase). This paper reports on the characterization of the molecular defects in 6 infantile patients from Turkish ancestry. Five of the 6 patients had reduced levels of the lysosomal a-glucosidase