Navigation Tabs STRUCTURES OF RANDOMLY GENERATED MUTANTS OF T4 LYSOZYME SHOW THAT PROTEIN STABILITY CAN BE ENHANCED BY RELAXATION OF STRAIN AND BY IMPROVED HYDROGEN BONDING VIA BOUND SOLVENT WebGL does not seem to be available.
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Sequence of 129L | STRUCTURES OF RANDOMLY GENERATED MUTANTS OF T4 LYSOZYME SHOW THAT PROTEIN STABILITY CAN BE ENHANCED BY RELAXATION OF STRAIN AND BY IMPROVED HYDROGEN BONDING VIA BOUND SOLVENT 129L | STRUCTURES OF RANDOMLY GENERATED MUTANTS OF T4 LYSOZYME SHOW THAT PROTEIN STABILITY CAN BE ENHANCED BY RELAXATION OF STRAIN AND BY IMPROVED HYDROGEN BONDING VIA BOUND SOLVENT Chain Polymers Everything 1: T4 LYSOZYME 2: CHLORIDE ION 3: BETA-MERCAPTOETHANOL 4: water A 1 M N I F E M L R I D 11 E G L R L K I Y K D 21 T E G Y Y T I G I G 31 H L L T K S P S L N 41 A A K S E L D K A I 51 G R N T N G V I T K 61 D E A E K L F N Q D 71 V D A A V R G I L R 81 N A K L K P V Y D S 91 L D T V R R A A L I 101 N M V F Q M G E T G 111 V A G F T N S L R M 121 L Q Q K R W D E A A 131 V N L A K S R W Y N 141 Q T P N R A K R V I 151 T T F R T G T W D A 161 Y K N L
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