Structure, stability, and chaperone function of αA-crystallin: Role of N-terminal region

Biopolymers ◽  
2007 ◽  
Vol 86 (3) ◽  
pp. 177-192 ◽  
Author(s):  
Madhuchhanda Kundu ◽  
P. C. Sen ◽  
K. P. Das
Keyword(s):  
Terminal Region ◽  
Structure Stability ◽  
Chaperone Function

scholarly journals Role of the carboxyl-terminal region of arrestin in binding to phosphorylated rhodopsin

1991 ◽  
Vol 266 (23) ◽  
pp. 15334-15339 ◽  
Author(s):  
K. Palczewski ◽  
J. Buczyłko ◽  
N.R. Imami ◽  
J.H. McDowell ◽  
P.A. Hargrave
Keyword(s):  
Terminal Region ◽  
Carboxyl Terminal

scholarly journals Role of the amino-terminal region of the DnaA protein in opening of the duplex DNA at theoriCregion

1999 ◽  
Vol 176 (1) ◽  
pp. 163-167 ◽  
Author(s):  
Shinji Mima ◽  
Yoshihiro Yamagachi ◽  
Taemi Kondo ◽  
Tomofusa Tsuchiya ◽  
Tohru Mizushima
Keyword(s):  
Terminal Region ◽  
Duplex Dna ◽  
Dnaa Protein ◽  
Amino Terminal

The role of the C-terminus and Kpn loop in the quaternary structure stability of nucleoside diphosphate kinase from Leishmania parasites

2015 ◽  
Vol 192 (3) ◽  
pp. 336-341 ◽  
Author(s):  
Plínio Salmazo Vieira ◽  
Priscila Oliveira de Giuseppe ◽  
Arthur Henrique Cavalcante de Oliveira ◽  
Mario Tyago Murakami
Keyword(s):  
Quaternary Structure ◽  
Nucleoside Diphosphate Kinase ◽  
Structure Stability ◽  
C Terminus ◽  
Leishmania Parasites

γ-Alumina: The Essential and Unexpected Role of Water for the Structure, Stability, and Reactivity of “Defect” Sites

2012 ◽  
Vol 134 (35) ◽  
pp. 14430-14449 ◽  
Author(s):  
Raphael Wischert ◽  
Pierre Laurent ◽  
Christophe Copéret ◽  
Françoise Delbecq ◽  
Philippe Sautet
Keyword(s):  
Structure Stability ◽  
Defect Sites

The role of the C-terminal region of olive latent virus 1 coat protein in host systemic infection

2006 ◽  
Vol 151 (10) ◽  
pp. 1973-1983 ◽  
Author(s):  
V. Pantaleo ◽  
F. Grieco ◽  
A. Di Franco ◽  
G. P. Martelli
Keyword(s):  
Coat Protein ◽  
Systemic Infection ◽  
Terminal Region ◽  
Latent Virus

Insight into structure, stability and hydrogen bond in complexes of guanine and thymine at the molecular level using computational chemical method

2021 ◽  
Vol 11 (1) ◽  
pp. 127-134
Author(s):  
Nhung Ngo Thi Hong ◽  
Huong Dau Thi Thu ◽  
Trung Nguyen Tien
Keyword(s):  
Hydrogen Bond ◽  
Hydrogen Bonds ◽  
Energy Surface ◽  
Covalent Bond ◽  
Electrostatic Energy ◽  
Substantial Contribution ◽  
Structure Stability ◽  
Dispersion Terms ◽  
Insight Into

Nine stable structures of complexes formed by interaction of guanine with thymine were located on potential energy surface at B3LYP/6-311++G(2d,2p). The complexes are quite stable with interaction energy from -5,8 to -17,7 kcal.mol-1. Strength of complexes are contributed by hydrogen bonds, in which a pivotal role of N−H×××O/N overcoming C−H×××O/N hydrogen bond, up to to 3.5 times, determines stabilization of complexes investigated. It is found that polarity of N/C−H covalent bond over proton affinity of N/O site governs stability of hydrogen bond in the complexes. The obtained results show that the N/C−H×××O/N red-shifting hydrogen bonds occur in all complexes, and a larger magnitude of an elongation of N−H compared C-H bond length accompanied by a decrease of its stretching frequency is detected in the N/C−H×××O/N hydrogen bond upon complexation. The SAPT2+ analysis indicates the substantial contribution of attractive electrostatic energy versus the induction and dispersion terms in stabilizing the complexes.

scholarly journals Effects of modifications of α-crystallin on its chaperone and other properties

2002 ◽  
Vol 364 (3) ◽  
pp. 711-717 ◽  
Author(s):  
Barry K. DERHAM ◽  
John J. HARDING
Keyword(s):  
Congenital Cataract ◽  
Point Mutations ◽  
Small Heat Shock Protein ◽  
High Molecular Mass ◽  
Lens Crystallins ◽  
Post Translational Modifications ◽  
Chaperone Function ◽  
Arginine Residues

The role of α-crystallin, a small heat-shock protein and chaperone, may explain how the lens stays transparent for so long. α-Crystallin prevents the aggregation of other lens crystallins and proteins that have become unfolded by ‘trapping’ the protein in a high-molecular-mass complex. However, during aging, the chaperone function of α-crystallin becomes compromised, allowing the formation of light-scattering aggregates that can proceed to form cataracts. Within the central part of the lens there is no turnover of damaged protein, and therefore post-translational modifications of α-crystallin accumulate that can reduce chaperone function; this is compounded in cataract lenses. Extensive in vitro glycation, carbamylation and oxidation all decrease chaperone ability. In the present study, we report the effect of the modifiers malondialdehyde, acetaldehyde and methylglyoxal, all of which are pertinent to cataract. Also modification by aspirin, which is known to delay cataract and other diseases, has been investigated. Recently, two point mutations of arginine residues were shown to cause congenital cataract. 1,2-Cyclohexanedione modifies arginine residues, and the extent of modification needed for a change in chaperone function was investigated. Only methylglyoxal and extensive modification by 1,2-cyclohexanedione caused a decrease in chaperone function. This highlights the robust nature of α-crystallin.

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