about
Removal of the Side Chain at the Active-Site Serine by a Glycine Substitution Increases the Stability of a Wide Range of Serine β-Lactamases by Relieving Steric StrainProtein stability: a crystallographer's perspectiveProlyl isomerization as a molecular memory in the allosteric regulation of the signal adapter protein c-CrkII.Sequential unfolding of the hemolysin two-partner secretion domain from Proteus mirabilis.Influence of V54M mutation in giant muscle protein titin: a computational screening and molecular dynamics approach.Molecular dynamics-based analyses of the structural instability and secondary structure of the fibrinogen gamma chain protein with the D356V mutation.Studying the role of cooperative hydration in stabilizing folded protein states.Forces stabilizing proteinsComputational tools help improve protein stability but with a solubility tradeoff.Global analysis of protein folding using massively parallel design, synthesis, and testing.Systematic analysis of residual density suggests that a major limitation in well-refined X-ray structures of proteins is the omission of ordered solvent.Estimation of the quality of refined protein crystal structures.Structure-Related Differences between Cytochrome Oxidase I Proteins in a Stable Heteroplasmic Mitochondrial System.Influences of lone-pair electrons on directionality of hydrogen bonds formed by hydrophilic amino acid side chains in molecular dynamics simulation.Alanine substitution in cellobiohydrolase provides new insights into substrate threading.Point mutation Arg153-His at surface of Bacillus lipase contributing towards increased thermostability and ester synthesis: insight into molecular network.Hydrophobic-hydrophilic forces in protein folding.Structural Studies of Predicted Ligand Binding Sites and Molecular Docking Analysis of Slc2a4 as a Therapeutic Target for the Treatment of Cancer.Assessing the effect of D59P mutation in the DE loop region in amyloid aggregation propensity of β2-microglobulin: A molecular dynamics simulation study.Constrained evolution of a bispecific enzyme: lessons for biocatalyst design.Structural Analysis of G1691S Variant in the Human Filamin B Gene Responsible for Larsen Syndrome: A Comparative Computational Approach.Redox-controlled self-inclusion of a lasso-type pseudo[1]rotaxane.Redesigning the type II' β-turn in green fluorescent protein to type I': implications for folding kinetics and stability.Accurate prediction of functional, structural, and stability changes in PITX2 mutations using in silico bioinformatics algorithms.Insight into novel clinical mutants of RpsA-S324F, E325K, and G341R of associated with pyrazinamide resistanceUsing a peptide segment to covalently conjugate doxorubicin and taxol for the study of drug combination effect
P2860
Q27704563-9B020871-D3A7-4AAC-9963-D85BF8CEDCE0Q28068775-C2EE0CA0-5555-4BFD-B91F-A4DE108F8AA3Q30009258-CE24FBBE-D0C1-43A3-8E3D-76AB6E882A33Q30152834-E8501529-BEF6-49E0-BFF4-A98A445982BBQ30387461-6C75B003-1883-4682-9601-A7385DA6A865Q30393472-CD566C42-BA3C-4F1F-9C34-CD7D8274C9DEQ37461059-FE1CFBE5-4487-48E7-B12F-EB04F2548253Q38213282-1CE04661-AE3B-4F3F-8150-01737ED9DFBDQ38678141-CE56DDBE-9086-4E59-A6C0-A4AB68BACB34Q38680071-D413086A-7ADA-4C81-9D12-AB9C55A96218Q38937897-32CA5401-E497-4793-A505-8FB6F5B212E8Q40295825-4F761EB2-77D4-4F3B-8F21-9A1F27B0C7F9Q46259529-BD8A1598-80CF-45DA-9DFE-9E9CFF160AE4Q47101907-BB298704-8756-4BD5-B834-3CF2550E85C8Q47130054-0683941B-FE4C-4470-B950-CE07B256CE49Q47585010-12007A19-3E79-4369-B276-3076DACF837EQ48042285-11D1D0FD-4D8F-45DD-9351-82AE3C0BEBACQ48043092-22B40A2C-16A8-47F3-AB38-5FBC036A89F0Q48058836-3D831F62-D173-4D67-B7C2-3D6674924FB9Q48093665-8E0B5EAE-F775-4F66-A20A-F182E60E0567Q48290136-97C705A3-1939-476F-9D76-5143B3488D75Q48308092-44FE8B54-18A2-4DB2-B760-6353E4C2F616Q50452689-307C3B95-177C-4758-AB78-A86FE5F2D513Q54981073-834E9B44-9010-45D3-A88E-B53B371BCAEBQ58583416-3037F987-8FF1-4993-AACD-C201D8830B47Q59279594-9FD5A4A1-118E-4A37-B01E-CC4EABD39703
P2860
description
2014 nî lūn-bûn
@nan
2014 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2014 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2014年の論文
@ja
2014年論文
@yue
2014年論文
@zh-hant
2014年論文
@zh-hk
2014年論文
@zh-mo
2014年論文
@zh-tw
2014年论文
@wuu
name
Contribution of hydrogen bonds to protein stability
@ast
Contribution of hydrogen bonds to protein stability
@en
Contribution of hydrogen bonds to protein stability
@nl
type
label
Contribution of hydrogen bonds to protein stability
@ast
Contribution of hydrogen bonds to protein stability
@en
Contribution of hydrogen bonds to protein stability
@nl
prefLabel
Contribution of hydrogen bonds to protein stability
@ast
Contribution of hydrogen bonds to protein stability
@en
Contribution of hydrogen bonds to protein stability
@nl
P2093
P2860
P3181
P356
P1433
P1476
Contribution of hydrogen bonds to protein stability
@en
P2093
Bret A Shirley
C Nick Pace
David Schell
Eric J Hebert
Gerald R Grimsley
Hailong Fu
J Martin Scholtz
Jeffery K Myers
John Landua
Jozef Sevcik
P2860
P304
P3181
P356
10.1002/PRO.2449
P577
2014-05-01T00:00:00Z