De novo structure generation using chemical shifts for proteins with high-sequence identity but different folds
about
Mutational Tipping Points for Switching Protein Folds and FunctionsCSI 2.0: a significantly improved version of the Chemical Shift Index.The role of negative selection in protein evolution revealed through the energetics of the native state ensemble.Aromatic claw: A new fold with high aromatic content that evades structural prediction.The NMR solution structure and function of RPA3313: a putative ribosomal transport protein from Rhodopseudomonas palustris.RosettaEPR: an integrated tool for protein structure determination from sparse EPR data.Systematic evaluation of CS-Rosetta for membrane protein structure prediction with sparse NOE restraints.Evolutionary dynamics on protein bi-stability landscapes can potentially resolve adaptive conflicts.Structure and dynamics of cationic membrane peptides and proteins: insights from solid-state NMR.An improved algorithm for MFR fragment assembly.Modeling proteins using a super-secondary structure library and NMR chemical shift informationSubdomain interactions foster the design of two protein pairs with ∼80% sequence identity but different folds.The albumin-binding domain as a scaffold for protein engineering.Implication of the cause of differences in 3D structures of proteins with high sequence identity based on analyses of amino acid sequences and 3D structures.Polymorphic triple beta-sheet structures contribute to amide hydrogen/deuterium (H/D) exchange protection in the Alzheimer amyloid beta42 peptideIdentification of helix capping and b-turn motifs from NMR chemical shiftsRecognition and cleavage of related to ubiquitin 1 (Rub1) and Rub1-ubiquitin chains by components of the ubiquitin-proteasome systemUtility of 1H NMR chemical shifts in determining RNA structure and dynamicsSmall-molecule ligand docking into comparative models with Rosetta.Practical aspects of NMR signal assignment in larger and challenging proteins.Protein dynamics and function from solution state NMR spectroscopy.Quantum chemical calculations of amide-15N chemical shift anisotropy tensors for a membrane-bound cytochrome-b5.Density functional calculations of backbone 15N shielding tensors in beta-sheet and turn residues of protein G.Local protein backbone folds determined by calculated NMR chemical shifts.Stabilization and structural analysis of a membrane-associated hIAPP aggregation intermediate.A Structurally Dynamic N-terminal Region Drives Function of the Staphylococcal Peroxidase Inhibitor (SPIN).Rapid measurement of residual dipolar couplings for fast fold elucidation of proteins.Molecular dynamics simulations on the conformational transitions from the GA 98 (GA 88) to GB 98 (GB 88) proteins.RDC derived protein backbone resonance assignment using fragment assembly.Examination of the quality of various force fields and solvation models for the equilibrium simulations of GA88 and GB88.Synthesis, antimicrobial activity and conformational analysis of the class IIa bacteriocin pediocin PA-1 and analogs thereof.
P2860
Q27677203-FE188B95-9F0F-4483-88A5-6C79904BCF01Q30367356-C23DC6D4-8B69-47D6-A5B5-56CB62A6B236Q30383783-A94A723D-99AC-4239-99A1-AA82D23FC5B1Q30394199-BBADB2DF-5599-4884-9AA3-66E3D7FD915DQ30394771-59C24581-A388-4206-8AD4-3F946210431AQ30395519-709479EE-0196-4082-98B5-0287C91FDF81Q30396232-DD7CE137-2483-4B4C-AF77-50A08D4F0CDDQ30421817-787262B2-2B18-4047-93AD-BF3234BC67F5Q33827462-DC968DFE-3606-4151-A1FD-CA3447BCFC78Q34267144-C63C29E3-8D9B-4965-95D9-5DA9583B9E3AQ34727938-6D7D9041-67E4-4FD8-A292-F64F6A15922AQ34863167-6BC18F75-378F-4ABA-84EB-657D30E036F6Q35136577-D41B0973-D890-42C8-937A-0CC98C09EBFBQ35260127-1D1D21E6-7432-4895-B273-FB8AC566D843Q35311079-02F5AC61-B760-4520-82ED-304284B839FAQ35977227-3BC87285-2478-465F-AB4B-E192134BF11AQ36455731-9585E876-411C-43BF-84D9-A217A92B7F23Q36914081-426CC051-F5D8-4F9F-A017-243EA4BE2BE5Q38112629-FFB3C877-5433-4A48-8114-D06E74CCE55DQ38188673-BFA29C94-962D-4405-AF0B-05A764FA7FC4Q38810874-AE82D614-334E-423B-A4B2-7BDACCC0552AQ42137311-529DC8FF-4C9C-4FF4-A84A-E94383F618C7Q42725118-4E669E9A-8BF7-4535-9AB1-6B2BF9DB06EBQ45810606-D9205CA4-E7CB-46D1-B9AB-30E59B0CA002Q46259687-8D9CC24E-B416-454D-B390-B3E942AEA8FEQ47227122-3ED942E4-E072-4285-8DE3-94B2AA6D3737Q51532353-81A117C0-2AF3-49C5-9858-6FD32384A449Q51601311-BDB6E062-DC3F-4F78-8B2F-6B4453E5C75FQ51620374-0F82A8B4-D658-4D71-BC12-04C7BFDD1950Q51654036-8C6ABCB9-44C4-466F-983D-16ADA514E5C1Q55383276-B229818E-F4A2-4172-A824-C86F4D69622E
P2860
De novo structure generation using chemical shifts for proteins with high-sequence identity but different folds
description
2010 nî lūn-bûn
@nan
2010 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
De novo structure generation u ...... e identity but different folds
@ast
De novo structure generation u ...... e identity but different folds
@en
type
label
De novo structure generation u ...... e identity but different folds
@ast
De novo structure generation u ...... e identity but different folds
@en
prefLabel
De novo structure generation u ...... e identity but different folds
@ast
De novo structure generation u ...... e identity but different folds
@en
P2093
P2860
P356
P1433
P1476
De novo structure generation u ...... e identity but different folds
@en
P2093
P2860
P304
P356
10.1002/PRO.303
P50
P577
2010-02-01T00:00:00Z