Differential scanning calorimetry as a tool for protein folding and stability

CM Johnson - Archives of biochemistry and biophysics, 2013 - Elsevier
Differential scanning calorimetry measures the heat capacity of states and the excess heat
associated with transitions that can be induced by temperature change. The integral of the …

Structure and function of α-crystallins: Traversing from in vitro to in vivo

M Haslbeck, J Peschek, J Buchner… - Biochimica et Biophysica …, 2016 - Elsevier
Background The two α-crystallins (αA-and αB-crystallin) are major components of our eye
lenses. Their key function there is to preserve lens transparency which is a challenging task …

Impact of structural stability of cold adapted Candida antarctica lipase B (CaLB): in relation to pH, chemical and thermal denaturation

G Rabbani, E Ahmad, MV Khan, MT Ashraf, R Bhat… - Rsc Advances, 2015 - pubs.rsc.org
The effect of pH on the conformational behavior of Candida antartica lipase B (CaLB) has
been monitored by spectroscopic and calorimetric studies. The results obtained from far and …

Promotion of protein solubility and reduction in stiffness in human lenses by aggrelyte-1: implications for reversing presbyopia

S Panja, H Gaikwad, J Rankenberg, MH Nam… - International Journal of …, 2023 - mdpi.com
With aging, human lenses lose the ability to focus on nearby objects due to decreases in
accommodative ability, a condition known as presbyopia. An increase in stiffness or …

Modulation of the structure and stability of novel camel lens alpha-crystallin by pH and thermal stress

A Malik, JM Khan, AS Alhomida, MS Ola - Gels, 2022 - mdpi.com
Alpha-crystallin protein performs structural and chaperone functions in the lens and
comprises alphaA and alphaB subunits at a molar ratio of 3: 1. The highly complex alpha …

Molecular mechanism of poly (vinyl alcohol) mediated prevention of aggregation and stabilization of insulin in nanoparticles

S Rawat, P Gupta, A Kumar, P Garg… - Molecular …, 2015 - ACS Publications
It is a challenge to formulate polymer based nanoparticles of therapeutic proteins as
excipients and process conditions affect stability and structural integrity of the protein …

Protection of ζ-crystallin by α-crystallin under thermal stress

A Malik, HA Almaharfi, JM Khan, M Hisamuddin… - International Journal of …, 2021 - Elsevier
Cataract is one of the major causes of blindness worldwide. Several factors including post-
translational modification, thermal and solar radiations promote cataractogenesis. The …

Conformational changes of α-crystallin proteins induced by heat stress

YY Chang, MH Hsieh, YC Huang, CJ Chen… - International Journal of …, 2022 - mdpi.com
α-crystallin is a major structural protein in the eye lenses of vertebrates that is composed of
two relative subunits, αA and αB crystallin, which function in maintaining lens transparency …

Control of the structural stability of α-crystallin under thermal and chemical stress: The role of carnosine

V Villari, F Attanasio, N Micali - The Journal of Physical Chemistry …, 2014 - ACS Publications
The structural properties of α-crystallin, the major protein of the eye lens of mammals, in
aqueous solution are investigated by means of small angle X-ray and dynamic light …

The synergistic chaperoning operation in a Bi-chaperone system consisting of alpha-crystallin and beta-casein: Bovine pancreatic insulin as the target protein

R Yousefi, S Jalili - Colloids and Surfaces B: Biointerfaces, 2011 - Elsevier
While chaperone activity of alpha-crystallin (α-Crs) is important in maintaining lens
transparency that of beta-casein (β-CN) is vital to prevent the development of corpora …