Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Nilesh Aghera"'
Autor:
Jayant B. Udgaonkar, Nilesh Aghera
Publikováno v:
Biochemistry. 56:3754-3769
Dissecting temporally the sequence of secondary structural changes, and determining how these specific changes modulate conformational heterogeneity, remain major goals of protein folding studies. In this study, the folding of the SH3 domain of PI3 k
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7b0f3c1a3b33b386f269e258fcbbe2e9
https://doi.org/10.1021/acs.biochem.7b00374
https://doi.org/10.1021/acs.biochem.7b00374
Autor:
Raghavan Varadarajan, Pankaj C. Jain, Siddharth Patel, Prasanth Kumar, Kritika Gupta, Shruti Khare, Ajai J. Pulianmackal, Nilesh Aghera, Arti Tripathi
Publikováno v:
Molecular Biology and Evolution
Understanding how mutations affect protein activity and organismal fitness is a major challenge. We used saturation mutagenesis combined with deep sequencing to determine mutational sensitivity scores for 1,664 single-site mutants of the 101 residue
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f7ead124b4d2832669834660e8781211
http://europepmc.org/articles/PMC5062330
http://europepmc.org/articles/PMC5062330
Autor:
Sneha Vishwanath, Himani Tandon, Narayanaswamy Srinivasan, Nilesh Aghera, Gopinath Chattopadhyay, Raghavan Varadarajan, Jyothi Prabha
Publikováno v:
Structure. 28:562-572.e4
Summary Most biological processes involve formation of transient complexes where binding of a ligand allosterically modulates function. The ccd toxin-antitoxin system is involved in plasmid maintenance and bacterial persistence. The CcdA antitoxin ac
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b6e205c6f9eac83a03dc01c68c003fde
https://doi.org/10.1016/j.str.2020.03.006
https://doi.org/10.1016/j.str.2020.03.006
Autor:
Nilesh Aghera, Chetana Baliga, Wolfgang E. Trommer, Raghavan Varadarajan, Siddhartha P. Sarma, Peter P. Borbat, Benjamin Selmke, Irina Worobiew
Publikováno v:
Biophysical journal. 116(5)
pH is an important factor that affects the protein structure, stability, and activity. Here, we probe the nature of the low-pH structural form of the homodimeric CcdB (controller of cell death B) protein. Characterization of CcdB protein at pH 4 and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::393864109716370f304044b5ba6ffe43
https://pubmed.ncbi.nlm.nih.gov/30777307
https://pubmed.ncbi.nlm.nih.gov/30777307
Autor:
Jayant B. Udgaonkar, Nilesh Aghera
Publikováno v:
Biochemistry. 52:5770-5779
Direct evidence of the presence of competing pathways for the folding or unfolding reactions of proteins is difficult to obtain. A direct signature for multiple pathways, seen so far only rarely in folding or unfolding studies, is an upward curvature
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1fa3bcef9e76ff6630b8dd1399b834e0
https://doi.org/10.1021/bi400688w
https://doi.org/10.1021/bi400688w
Publikováno v:
Biochemistry. 55(43)
The existence of parallel pathways in the folding of proteins seems intuitive, yet remains controversial. We explore the folding kinetics of the homodimeric Escherichia coli toxin CcdB (Controller of Cell Division or Death B protein) using multiple o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::205a8d6a4a46fedf94c19b2b3ac73d1b
https://pubmed.ncbi.nlm.nih.gov/27696818
https://pubmed.ncbi.nlm.nih.gov/27696818
Publikováno v:
Biochemistry. 51:9058-9066
A buried ionizable residue can have a drastic effect on the stability of a native protein, but there has been only limited investigation of how burial of an ionizable residue affects the kinetics of protein folding. In this study, the effect of buria
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a1a605f6f179cd0a209a706cc88c4d51
https://doi.org/10.1021/bi3008017
https://doi.org/10.1021/bi3008017
Autor:
Jayant B. Udgaonkar, Nilesh Aghera
Publikováno v:
Protein Expression and Purification. 76:248-253
Monellin is an intensely sweet-tasting protein present in the berry of Dioscoreophyllum cumminsii. Naturally occurring monellin (double chain monellin) is a heterodimer of two subunits commonly referred to as chain A and chain B. Monellin is a good m
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1594ffc29e7b9f774f45086f95efade8
https://doi.org/10.1016/j.pep.2010.11.002
https://doi.org/10.1016/j.pep.2010.11.002
Autor:
Nilesh Aghera, Jayant B. Udgaonkar
Publikováno v:
Journal of molecular biology. 420(3)
Determining whether or not a protein uses multiple pathways to fold is an important goal in protein folding studies. When multiple pathways are present, defined by transition states that differ in their compactness and structure but not significantly
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3d063147df35182b5115a54b2685fdf7
https://pubmed.ncbi.nlm.nih.gov/22542529
https://pubmed.ncbi.nlm.nih.gov/22542529
Publikováno v:
Biochemistry. 50(13)
To improve our understanding of the contributions of different stabilizing interactions to protein stability, including that of residual structure in the unfolded state, the small sweet protein monellin has been studied in both its two variant forms,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a00c8e9054f9f247109db8567d014796
https://pubmed.ncbi.nlm.nih.gov/21351752
https://pubmed.ncbi.nlm.nih.gov/21351752