Toward a simplification of the protein folding problem: a stabilizing polyalanine .alpha.-helix engineered in T4 lysozyme

Biochemistry ◽  
1991 ◽  
Vol 30 (8) ◽  
pp. 2012-2017 ◽  
Author(s):  
X. J. Zhang ◽  
W. A. Baase ◽  
B. W. Matthews
Keyword(s):  
Protein Folding ◽  
Alpha Helix ◽  
T4 Lysozyme

Analysis of the interaction between charged side chains and the .alpha.-helix dipole using designed thermostable mutants of phage T4 lysozyme

Biochemistry ◽  
1991 ◽  
Vol 30 (41) ◽  
pp. 9816-9828 ◽  
Author(s):  
H. Nicholson ◽  
D. E. Anderson ◽  
S. Dao Pin ◽  
B. W. Matthews
Keyword(s):  
Alpha Helix ◽  
Side Chains ◽  
T4 Lysozyme ◽  
Phage T4

Replacements of Pro86 in phage T4 lysozyme extend an alpha-helix but do not alter protein stability

Science ◽  
1988 ◽  
Vol 239 (4840) ◽  
pp. 631-635 ◽  
Author(s):  
T Alber ◽  
J. Bell ◽  
D. Sun ◽  
H Nicholson ◽  
J. Wozniak ◽  
...  
Keyword(s):  
Protein Stability ◽  
Alpha Helix ◽  
T4 Lysozyme ◽  
Phage T4

scholarly journals Modulating long-range energetics via helix stabilization: a case study using T4 lysozyme

2018 ◽  
Author(s):  
Sabriya N. Rosemond ◽  
Kambiz M. Hamadani ◽  
Jamie H.D. Cate ◽  
Susan Marqusee
Keyword(s):  
Protein Folding ◽  
Long Range ◽  
Salt Bridge ◽  
Globular Protein ◽  
Full Length ◽  
T4 Lysozyme ◽  
Long Distance ◽  
Terminal Fragment ◽  
The Stability

Cooperative protein folding requires distant regions of a protein to interact and provide mutual stabilization. The mechanism of this long-distance coupling remains poorly understood. Here, we use T4 lysozyme (T4L*) as a model to investigate long-range communications across a globular protein. T4L* is composed of two structurally distinct subdomains, although it behaves in a two-state manner at equilibrium. The subdomains of T4L* are connected via two topological connections: the N-terminal helix that is structurally part of the C-terminal subdomain (the A-helix) and a long helix that spans both subdomains (the C-helix). To understand the role that the C-helix plays in cooperative folding, we analyzed a circularly permuted version of T4L* (CP13*), whose subdomains are connected only by the C-helix. We demonstrate that when isolated as individual fragments, both subdomains of CP13* can fold autonomously into marginally stable conformations. The energetics of the N-terminal subdomain depend on the formation of a salt bridge known to be important for stability in the full-length protein. We show that the energetic contribution of the salt bridge to the stability of the N-terminal fragment increases when the C-helix is stabilized, such as occurs upon folding of the C-terminal subdomain. These results suggest a model where long-range energetic coupling is mediated by helix stabilization.

Hierarchical strategy for protein folding and design: synthesis and expression of T4 lysozyme gene and two putative folding mutants

1987 ◽  
Vol 1 (6) ◽  
pp. 481-485 ◽  
Author(s):  
S.A. Narang ◽  
Fei-Long Yao ◽  
J.J. Michniewicz ◽  
G. Dubuc ◽  
J. Phipps ◽  
...  
Keyword(s):  
Protein Folding ◽  
T4 Lysozyme ◽  
Design Synthesis ◽  
Lysozyme Gene

Simple, yet powerful methodologies for conformational sampling of proteins

2015 ◽  
Vol 17 (9) ◽  
pp. 6155-6173 ◽  
Author(s):  
Ryuhei Harada ◽  
Yu Takano ◽  
Takeshi Baba ◽  
Yasuteru Shigeta
Keyword(s):  
Protein Folding ◽  
Large Amplitude ◽  
Sampling Methods ◽  
Substrate Binding ◽  
Conformational Sampling ◽  
T4 Lysozyme ◽  
Induced Fit ◽  
Feature Article ◽  
Loop Region ◽  
Small Proteins

This feature article reviews four different conformational sampling methods for proteins recently developed by us. We here deal with protein folding of small proteins, large amplitude domain motion of T4 lysozyme, and induced-fit motion of a loop region after substrate binding using our methods.

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