[NMR paper] Salt Dependence Conformational Stability of the Dimeric SAM Domain of MAPKKK Ste11 from Budding Yeast: A Native State H/D Exchange NMR Study".
Related ArticlesSalt Dependence Conformational Stability of the Dimeric SAM Domain of MAPKKK Ste11 from Budding Yeast: A Native State H/D Exchange NMR Study".
Biochemistry. 2020 Jul 15;:
Authors: Bhunia A, Ilyas H, Bhattacharjya S
Abstract
The sterile ? motif, also called the SAM domain, is known to form homo or heterocomplexes that modulate diverse biological functions through regulation of specific protein-protein interactions. The MAPK pathway of budding yeast Saccharomyces cerevisiae comprises a three-tier kinase system akin to mammals. The MAPKKK Ste11 protein of yeast contains a homodimer SAM domain, which is critical for transmitting cues to the downstream kinases. The structural stability of the dimeric Ste11 SAM is maintained by hydrophobic and ionic interactions at the interfacial amino acids. Urea induced equilibrium unfolding process of the Ste11 SAM domain is cooperative without evidence of any intermediate states. The native state H/D exchange under sub-denaturing conditions is a useful method for the detection of intermediate states of proteins. In the present study, we investigated the effect of ionic strength on the conformational stability of the dimer using the H/D exchange study. The hydrogen exchange behavior of the Ste11 dimer under physiological salt concentration reveals two metastable partially folded intermediate states, which may be generated by a sequential and cooperative unfolding of the five helices of the fold. These intermediates appear to be the dominant species for the dynamic and reversible unfolding of the Ste11 SAM domain, underlining a significant pathway for its folding kinetics via hydrophobic collapse. In contrast, higher ionic concentration eliminates this cooperativity between the stabilizing pairs of helices.
PMID: 32667811 [PubMed - as supplied by publisher]
[NMR paper] Characterization of the near native conformational states of the SAM domain of Ste11 protein by NMR spectroscopy.
Characterization of the near native conformational states of the SAM domain of Ste11 protein by NMR spectroscopy.
Related Articles Characterization of the near native conformational states of the SAM domain of Ste11 protein by NMR spectroscopy.
Proteins. 2014 Jul 26;
Authors: Gupta S, Bhattacharjya S
Abstract
The sterile alpha motif or SAM domain is one of the most frequently present protein interaction modules with diverse functional attributions. SAM domain of the Ste11 protein of budding yeast plays important roles in...
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07-30-2014 10:22 AM
[NMR paper] Studying "Invisible" Excited Protein States in Slow Exchange with a Major State Conformation.
From Mendeley Biomolecular NMR group:
Studying "Invisible" Excited Protein States in Slow Exchange with a Major State Conformation.
Journal of the American Chemical Society (2012). Pramodh Vallurupalli, Guillaume Bouvignies, Lewis E Kay et al.
Ever since its initial development, solution NMR spectroscopy has been used as a tool to study conformational exchange. Although many systems are amenable to relaxation dispersion approaches, cases involving highly skewed populations in slow chemical exchange have, in general, remained recalcitrant to study. Here an experiment to detect and...
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10-17-2013 12:49 PM
[NMR paper] Clusters of Branched Aliphatic Side Chains Serve As Cores of Stability in the Native State of the HisF TIM Barrel Protein.
Clusters of Branched Aliphatic Side Chains Serve As Cores of Stability in the Native State of the HisF TIM Barrel Protein.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Clusters of Branched Aliphatic Side Chains Serve As Cores of Stability in the Native State of the HisF TIM Barrel Protein.
J Mol Biol. 2013 Jan 16;
Authors: Gangadhara BN, Laine JM, Kathuria SV, Massi F, Matthews CR
Abstract
Imidazole-3-glycerol phosphate synthase is a heterodimeric allosteric...
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02-03-2013 10:19 AM
[NMR paper] Studying "Invisible" Excited Protein States in Slow Exchange with a Major State Conformation.
From Mendeley Biomolecular NMR group:
Studying "Invisible" Excited Protein States in Slow Exchange with a Major State Conformation.
Journal of the American Chemical Society (2012). Pramodh Vallurupalli, Guillaume Bouvignies, Lewis E Kay et al.
Ever since its initial development, solution NMR spectroscopy has been used as a tool to study conformational exchange. Although many systems are amenable to relaxation dispersion approaches, cases involving highly skewed populations in slow chemical exchange have, in general, remained recalcitrant to study. Here an experiment to detect and...
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11-12-2012 01:53 AM
[NMR paper] Studying "Invisible" Excited Protein States in Slow Exchange with a Major State Conformation.
From Mendeley Biomolecular NMR group:
Studying "Invisible" Excited Protein States in Slow Exchange with a Major State Conformation.
Journal of the American Chemical Society (2012). Pramodh Vallurupalli, Guillaume Bouvignies, Lewis E Kay et al.
Ever since its initial development, solution NMR spectroscopy has been used as a tool to study conformational exchange. Although many systems are amenable to relaxation dispersion approaches, cases involving highly skewed populations in slow chemical exchange have, in general, remained recalcitrant to study. Here an experiment to detect and...
nmrlearner
Journal club
0
10-12-2012 09:58 AM
[NMR paper] Studying "Invisible" Excited Protein States in Slow Exchange with a Major State Conformation.
From Mendeley Biomolecular NMR group:
Studying "Invisible" Excited Protein States in Slow Exchange with a Major State Conformation.
Journal of the American Chemical Society (2012). Pramodh Vallurupalli, Guillaume Bouvignies, Lewis E Kay et al.
Ever since its initial development, solution NMR spectroscopy has been used as a tool to study conformational exchange. Although many systems are amenable to relaxation dispersion approaches, cases involving highly skewed populations in slow chemical exchange have, in general, remained recalcitrant to study. Here an experiment to detect and...
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08-24-2012 08:01 PM
[NMR paper] Ribonuclease Sa conformational stability studied by NMR-monitored hydrogen exchange.
Ribonuclease Sa conformational stability studied by NMR-monitored hydrogen exchange.
Related Articles Ribonuclease Sa conformational stability studied by NMR-monitored hydrogen exchange.
Biochemistry. 2005 May 31;44(21):7644-55
Authors: Laurents DV, Scholtz JM, Rico M, Pace CN, Bruix M
The conformational stability of ribonuclease Sa (RNase Sa) has been measured at the per-residue level by NMR-monitored hydrogen exchange at pH* 5.5 and 30 degrees C. In these conditions, the exchange mechanism was found to be EXII. The conformational stability...
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11-25-2010 08:21 PM
[NMR paper] Microscopic stability of cold shock protein A examined by NMR native state hydrogen e
Microscopic stability of cold shock protein A examined by NMR native state hydrogen exchange as a function of urea and trimethylamine N-oxide.
Related Articles Microscopic stability of cold shock protein A examined by NMR native state hydrogen exchange as a function of urea and trimethylamine N-oxide.
Protein Sci. 2000 Feb;9(2):290-301
Authors: Jaravine VA, Rathgeb-Szabo K, Alexandrescu AT
Native state hydrogen exchange of cold shock protein A (CspA) has been characterized as a function of the denaturant urea and of the stabilizing agent...
Salt Dependence Conformational Stability of the Dimeric SAM Domain of MAPKKK Ste11 from Budding Yeast: A Native State H/D Exchange NMR Study".
Linear Mode
