Brandon L Kier
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Explore the profile of Brandon L Kier including associated specialties, affiliations and a list of published articles.
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23
Citations
201
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Recent Articles
1.
Reback M, Ginovska B, Buchko G, Dutta A, Priyadarshani N, Kier B, et al.
J Coord Chem
. 2020 Oct;
69(11-13):1730-1747.
PMID: 33093711
Building on our recent report of an active H production catalyst [Ni(P N)] (Prop = phenylpropionic acid, peptide (R10) = WIpPRWTGPR-NH, p = D-proline and PN = 1-aza-3,6-diphosphacycloheptane) that contains...
2.
Sivanesam K, Kier B, Whedon S, Chatterjee C, Andersen N
J Pept Sci
. 2017 Dec;
23(12):899-906.
PMID: 29193517
Designing new antimicrobial peptides (AMPs) focuses heavily on the activity of the peptide and less on the elements that stabilize the secondary structure of these peptides. Studies have shown that...
3.
Ge Y, Kier B, Andersen N, Voelz V
J Chem Inf Model
. 2017 Jun;
57(7):1609-1620.
PMID: 28614661
Molecular simulation has been used to model the detailed folding properties of peptides, yet prospective computational peptide design by such approaches remains challenging and nontrivial. To test the accuracy of...
4.
Sivanesam K, Kier B, Whedon S, Chatterjee C, Andersen N
FEBS Lett
. 2016 Nov;
590(24):4480-4488.
PMID: 27859052
Many naturally occurring antimicrobial peptides (AMPs) are amphipathic with a β-hairpin conformation stabilized by cross-strand disulfides across the associated β-strands. Here, we show that the disulfides are not essential. Other...
5.
Anderson J, Shcherbakov A, Kier B, Kellock J, Shu I, Byrne A, et al.
Biopolymers
. 2016 Oct;
107(3).
PMID: 27701729
Protein loops make up a large portion of the secondary structure in nature. But very little is known concerning loop closure dynamics and the effects of loop composition on fold...
6.
Anderson J, Kier B, Jurban B, Byrne A, Shu I, Eidenschink L, et al.
Biopolymers
. 2016 Feb;
105(6):337-356.
PMID: 26850220
We have extended our studies of Trp/Trp to other Aryl/Aryl through-space interactions that stabilize hairpins and other small polypeptide folds. Herein we detail the NMR and CD spectroscopic features of...
7.
Kier B, Newbloom G, Pozzo L, Andersen N
Chembiochem
. 2015 Nov;
17(3):224-7.
PMID: 26603832
Beta sheets are inherently length-limited; adding residues to the ends of model β-sheets does not necessarily grow the β-sheet. Here, we present a method for extending β-sheets to any length...
8.
Meadows C, Balakrishnan G, Kier B, Spiro T, Klinman J
J Am Chem Soc
. 2015 Jul;
137(32):10060-3.
PMID: 26223665
Protein dynamics on the microsecond (μs) time scale were investigated by temperature-jump fluorescence spectroscopy as a function of temperature in two variants of a thermophilic alcohol dehydrogenase: W87F and W87F:H43A....
9.
Kier B, Anderson J, Andersen N
J Am Chem Soc
. 2015 Apr;
137(16):5363-71.
PMID: 25835058
Disulfide bonds between cysteine residues are essential to the structure and folding of many proteins. Yet their role in the design of structured peptides and proteins has frequently been limited...
10.
Anderson J, Kier B, Shcherbakov A, Andersen N
FEBS Lett
. 2014 Dec;
588(24):4749-53.
PMID: 25451230
Understanding protein beta structures has been hindered by the challenge of designing small, well-folded β-sheet systems. A β-capping motif was previously designed to help solve this problem, but not without...